Performance information

• Production of extracellular superoxide contributes to photosynthesis via elimination of reducing power and regeneration of NADP+ in the red-tide-forming raphidophyte Chattonella marina complex　　　　　　　　　　　　　　　
  Koki Yuasa; Takayoshi Ichikawa; Yuma Ishikawa; Haruhiko Jimbo; Maki Kawai-Yamada; Tomoyuki Shikata; Yoshitaka Nishiyama
  Harmful Algae, Volume：139, First page：102712, Last page：102712, Sep. 2024, [Reviewed], [Corresponding]
  Elsevier BV, Scientific journal
  DOI：https://doi.org/10.1016/j.hal.2024.102712
  DOI ID：10.1016/j.hal.2024.102712, ISSN：1568-9883, 共同研究・競争的資金等ID：48384882;35751341
• The toxigenic red-tide-forming dinoflagellates Alexandrium leei and Alexandrium catenella differ in terms of the sensitivity to strong light and low temperature of their photosynthetic machinery　　　　　　　　　　　　　　　
  Atsuki Suka; Tomoyuki Shikata; Koki Yuasa; Yuji Tomaru; Pornpan Napaumpaiporn; Ryusuke Tanaka; Yoshitaka Nishiyama
  Algal Research, Volume：79, First page：103495, Last page：103495, Apr. 2024, [Reviewed], [Corresponding]
  Elsevier BV, Scientific journal
  DOI：https://doi.org/10.1016/j.algal.2024.103495
  DOI ID：10.1016/j.algal.2024.103495, ISSN：2211-9264, 共同研究・競争的資金等ID：48384882;35751341
• Improved capacity for the repair of photosystem II via reinforcement of the translational and antioxidation systems in Synechocystis sp. PCC 6803
  Pornpan Napaumpaiporn; Takako Ogawa; Kintake Sonoike; Yoshitaka Nishiyama
  The Plant Journal, Feb. 2024, [Reviewed], [Corresponding]
  SUMMARY
  
  In the cyanobacterium Synechocystis sp. PCC 6803, translation factor EF‐Tu is inactivated by reactive oxygen species (ROS) via oxidation of Cys82 and the oxidation of EF‐Tu enhances the inhibition of the repair of photosystem II (PSII) by suppressing protein synthesis. In our present study, we generated transformants of Synechocystis that overexpressed a mutated form of EF‐Tu, designated EF‐Tu (C82S), in which Cys82 had been replaced by a Ser residue, and ROS‐scavenging enzymes individually or together. Expression of EF‐Tu (C82S) alone in Synechocystis enhanced the repair of PSII under strong light, with the resultant mitigation of PSII photoinhibition, but it stimulated the production of ROS. However, overexpression of superoxide dismutase and catalase, together with the expression of EF‐Tu (C82S), lowered intracellular levels of ROS and enhanced the repair of PSII more significantly under strong light, via facilitation of the synthesis de novo of the D1 protein. By contrast, the activity of photosystem I was hardly affected in wild‐type cells and in all the lines of transformed cells under the same strong‐light conditions. Furthermore, transformed cells that overexpressed EF‐Tu (C82S), superoxide dismutase, and catalase were able to survive longer under stronger light than wild‐type cells. Thus, the reinforced capacity for both protein synthesis and ROS scavenging allowed both photosynthesis and cell proliferation to tolerate strong light.
  Wiley, English, Scientific journal
  DOI：https://doi.org/10.1111/tpj.16551
  DOI ID：10.1111/tpj.16551, ISSN：0960-7412, eISSN：1365-313X, 共同研究・競争的資金等ID：43652948
• Light Influences the Growth, Pigment Synthesis, Photosynthesis Capacity, and Antioxidant Activities in Scenedesmus falcatus
  Rattanaporn Songserm; Yoshitaka Nishiyama; Nuttha Sanevas
  Scientifica, Volume：2024, First page：1, Last page：12, Jan. 2024, [Reviewed]
  Light plays a significant role in microalgae cultivation, significantly influencing critical parameters, including biomass production, pigment content, and the accumulation of metabolic compounds. This study was intricately designed to optimize light intensities, explicitly targeting enhancing growth, pigmentation, and antioxidative properties in the green microalga, Scenedesmus falcatus (KU.B1). Additionally, the study delved into the photosynthetic efficiency in light responses of S. falcatus. The cultivation of S. falcatus was conducted in TRIS-acetate-phosphate medium (TAP medium) under different light intensities of 100, 500, and 1000 μmol photons m−2·s−1 within a photoperiodic cycle of 12 h of light and 12 h of dark. Results indicated a gradual increase in the growth of S. falcatus under high light conditions at 1000 μmol photons m−2·s−1, reaching a maximum optical density of 1.33 ± 0.03 and a total chlorophyll content of 22.67 ± 0.2 μg/ml at 120 h. Conversely, a slower growth rate was observed under low light at 100 μmol photons m−2·s−1. However, noteworthy reductions in the maximum quantum yield (Fv/Fm) and actual quantum yield (Y(II)) were observed under 1000 μmol photons m−2·s−1, reflecting a decline in algal photosynthetic efficiency. Interestingly, these changes under 1000 μmol photons m−2·s−1 were concurrent with a significant accumulation of a high amount of beta-carotene (919.83 ± 26.33 mg/g sample), lutein (34.56 ± 0.19 mg/g sample), and canthaxanthin (24.00 ± 0.38 mg/g sample) within algal cells. Nevertheless, it was noted that antioxidant activities and levels of total phenolic compounds (TPCs) decreased under high light at 1000 μmol photons m−2·s−1, with IC50 of DPPH assay recorded at 218.00 ± 4.24 and TPC at 230.83 ± 86.75 mg of GAE/g. The findings suggested that the elevated light intensity at 1000 μmol photons m−2·s−1 enhanced the growth and facilitated the accumulation of valuable carotenoid pigment in S. falcatus, presenting potential applications in the functional food and carotenoid industry.
  Hindawi Limited, Scientific journal
  DOI：https://doi.org/10.1155/2024/1898624
  DOI ID：10.1155/2024/1898624, eISSN：2090-908X
• Chloroplast translation factor EF-Tu of Arabidopsis thaliana can be inactivated via oxidation of a specific cysteine residue
  Machi Toriu; Momoka Horie; Yuka Kumaki; Taku Yoneyama; Shin Kore-eda; Susumu Mitsuyama; Keisuke Yoshida; Toru Hisabori; Yoshitaka Nishiyama
  Biochemical Journal, Feb. 2023, [Reviewed], [Corresponding]
  Translational elongation factor EF-Tu, which delivers aminoacyl-tRNA to the ribosome, is susceptible to inactivation by reactive oxygen species (ROS) in the cyanobacterium Synechocystis sp. PCC 6803. However, the sensitivity to ROS of chloroplast-localized EF-Tu (cpEF-Tu) of plants remains to be elucidated. In the present study, we generated a recombinant cpEF-Tu protein of Arabidopsis thaliana and examined its sensitivity to ROS in vitro. In cpEF-Tu that lacked a bound nucleotide, one of the two cysteine residues, Cys149 and Cys451, in the mature protein was sensitive to oxidation by H2O2, with the resultant formation of sulfenic acid. The translational activity of cpEF-Tu, as determined with an in vitro translation system, derived from Escherichia coli, that had been reconstituted without EF-Tu, decreased with the oxidation of a cysteine residue. Replacement of Cys149 with an alanine residue rendered cpEF-Tu insensitive to inactivation by H2O2, indicating that Cys149 might be the target of oxidation. By contrast, cpEF-Tu that had bound either GDP or GTP was less sensitive to oxidation by H2O2 than nucleotide-free cpEF-Tu. Addition of thioredoxin f1, a major thioredoxin in the Arabidopsis chloroplast, to oxidized cpEF-Tu allowed the reduction of Cys149 and the reactivation of cpEF-Tu, suggesting that the oxidation of cpEF-Tu might be a reversible regulatory mechanism that suppresses the chloroplast translation system in a redox-dependent manner.
  Portland Press Ltd., Scientific journal
  DOI：https://doi.org/10.1042/bcj20220609
  DOI ID：10.1042/bcj20220609, ISSN：0264-6021, eISSN：1470-8728, 共同研究・競争的資金等ID：43652948;49618172;35751334
• Recovery of photosynthesis after long-term storage in the terrestrial cyanobacterium Nostoc commune.　　　　　　　　　　　　　　　
  Toshio Sakamoto; Yang Wei; Koki Yuasa; Yoshitaka Nishiyama
  The Journal of general and applied microbiology, May 2022, ［Domestic magazine］
  The terrestrial cyanobacterium Nostoc commune is an anhydrobiotic organism with extreme longevity. Recovery of photosynthesis by rehydration was examined using our laboratory stocks of dry N. commune thalli after long-term storage in a desiccated state. In the samples stored at room temperature for over 8 years, photosynthetic oxygen evolution was barely detectable, whereas oxygen consumption was recovered. There was an exceptional case in which photosynthetic oxygen evolution recovered after 8 years of storage at room temperature. Both photosynthetic oxygen evolution and respiratory oxygen consumption were recovered in dry thalli stored at -20°C for over 15 years. Consistent with the recovery of photosynthetic oxygen evolution, Fv/Fm was detected in the samples stored at -20°C at levels similar to those of freshly collected N. commune colonies. Carotenoids, scytonemin and chlorophyll a appeared to be intact in the dry thalli stored at -20°C, but β-carotene was not detected in the samples stored at room temperature. α-Tocopherol was intact in the samples stored at -20°C but was degraded in the samples stored at room temperature. These results suggest that dry thalli of N. commune are capable of sustaining biological activities for a long time, although they are gradually damaged when stored at room temperature.
  English, Scientific journal
  DOI：https://doi.org/10.2323/jgam.2022.01.003
  DOI ID：10.2323/jgam.2022.01.003, PubMed ID：35598979
• Superoxide Production by the Red Tide-Producing Chattonella marina Complex (Raphidophyceae) Correlates with Toxicity to Aquacultured Fishes
  Tomoyuki Shikata; Koki Yuasa; Saho Kitatsuji; Setsuko Sakamoto; Kazuki Akita; Yuichiro Fujinami; Yoshitaka Nishiyama; Toshihisa Kotake; Ryusuke Tanaka; Yasuhiro Yamasaki
  Antioxidants, Volume：10, Number：10, First page：1635, Last page：1635, Oct. 2021, [Reviewed]
  The marine raphidophyte Chattonella marina complex forms red tides, causing heavy mortalities of aquacultured fishes in temperate coastal waters worldwide. The mechanism for Chattonella fish mortality remains unresolved. Although several toxic chemicals have been proposed as responsible for fish mortality, the cause is still unclear. In this study, we performed toxicity bioassays with red sea bream and yellowtail. We also measured biological parameters potentially related to ichthyotoxicity, such as cell size, superoxide (O2•−) production, and compositions of fatty acids and sugars, in up to eight Chattonella strains to investigate possible correlations with toxicity. There were significant differences in moribundity rates of fish and in all biological parameters among strains. One strain displayed no ichthyotoxicity even at high cell densities. Strains were categorized into three groups based on cell length, but this classification did not significantly correlate with ichthyotoxicity. O2•− production differed by a factor of more than 13 between strains at the late exponential growth phase. O2•− production was significantly correlated with ichthyotoxicity. Differences in fatty acid and sugar contents were not related to ichthyotoxicity. Our study supports the hypothesis that superoxide can directly or indirectly play an important role in the Chattonella-related mortality of aquacultured fishes.
  MDPI AG, Scientific journal
  DOI：https://doi.org/10.3390/antiox10101635
  DOI ID：10.3390/antiox10101635, eISSN：2076-3921
• The NAD Kinase Slr0400 Functions as a Growth Repressor in Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  Yuuma Ishikawa; Cedric Cassan; Aikeranmu Kadeer; Koki Yuasa; Nozomu Sato; Kintake  Sonoike; Yasuko Kaneko; Atsuko Miyagi; Hiroko Takahashi; Toshiki Ishikawa; Masatoshi Yamaguchi; Yoshitaka Nishiyama; Yukako Hihara; Yves Gibon; Maki Kawai-Yamada
  Plant and Cell Physiology, Volume：62, Number：4, First page：668, Last page：677, Sep. 2021, [Reviewed]
  
  NADP+, the phosphorylated form of nicotinamide adenine dinucleotide (NAD), plays an essential role in many cellular processes. NAD kinase (NADK), which is conserved in all living organisms, catalyzes the phosphorylation of NAD+ to NADP+. However, the physiological role of phosphorylation of NAD+ to NADP+ in the cyanobacterium Synechocystis remains unclear. In this study, we report that slr0400, an NADK-encoding gene in Synechocystis, functions as a growth repressor under light-activated heterotrophic growth conditions and light and dark cycle conditions in the presence of glucose. We show, via characterization of NAD(P)(H) content and enzyme activity, that NAD+ accumulation in slr0400-deficient mutant results in the unsuppressed activity of glycolysis and tricarboxylic acid (TCA) cycle enzymes. In determining whether Slr0400 functions as a typical NADK, we found that constitutive expression of slr0400 in an Arabidopsis nadk2-mutant background complements the pale-green phenotype. Moreover, to determine the physiological background behind the growth advantage of mutants lacking slr04000, we investigated the photobleaching phenotype of slr0400-deficient mutant under high-light conditions. Photosynthetic analysis found in the slr0400-deficient mutant resulted from malfunctions in the Photosystem II (PSII) photosynthetic machinery. Overall, our results suggest that NADP(H)/NAD(H) maintenance by slr0400 plays a significant role in modulating glycolysis and the TCA cycle to repress the growth rate and maintain the photosynthetic capacity.
  Oxford University Press (OUP), Scientific journal
  DOI：https://doi.org/10.1093/pcp/pcab023
  DOI ID：10.1093/pcp/pcab023, ISSN：0032-0781, eISSN：1471-9053, PubMed ID：33210985, PubMed Central ID：PMC7781788
• Dissection of the Mechanisms of Growth Inhibition Resulting from Loss of the PII Protein in the Cyanobacterium Synechococcus elongatus PCC 7942　　　　　　　　　　　　　　　
  Takayuki Sakamoto; Nobuyuki Takatani; Kintake Sonoike; Haruhiko Jimbo; Yoshitaka Nishiyama; Tatsuo Omata
  Plant and Cell Physiology, Volume：62, Number：4, First page：721, Last page：731, Sep. 2021, [Reviewed]
  
  In cyanobacteria, the PII protein (the glnB gene product) regulates a number of proteins involved in nitrogen assimilation including PipX, the coactivator of the global nitrogen regulator protein NtcA. In Synechococcus elongatus PCC 7942, construction of a PII-less mutant retaining the wild-type pipX gene is difficult because of the toxicity of uncontrolled action of PipX and the other defect(s) resulting from the loss of PIIper se, but the nature of the PipX toxicity and the PipX-independent defect(s) remains unclear. Characterization of a PipX-less glnB mutant (PD4) in this study showed that the loss of PII increases the sensitivity of PSII to ammonium. Ammonium was shown to stimulate the formation of reactive oxygen species in the mutant cells. The ammonium-sensitive growth phenotype of PD4 was rescued by the addition of an antioxidant α-tocopherol, confirming that photo-oxidative damage was the major cause of the growth defect. A targeted PII mutant retaining wild-type pipX was successfully constructed from the wild-type S. elongatus strain (SPc) in the presence of α-tocopherol. The resulting mutant (PD1X) showed an unusual chlorophyll fluorescence profile, indicating extremely slow reduction and re-oxidation of QA, which was not observed in mutants defective in both glnB and pipX. These results showed that the aberrant action of uncontrolled PipX resulted in an impairment of the electron transport reactions in both the reducing and oxidizing sides of QA.
  Oxford University Press (OUP), Scientific journal
  DOI：https://doi.org/10.1093/pcp/pcab030
  DOI ID：10.1093/pcp/pcab030, ISSN：0032-0781, eISSN：1471-9053, PubMed ID：33650637
• Nutrient deficiency stimulates the production of superoxide in the noxious red-tide-forming raphidophyte Chattonella antiqua　　　　　　　　　　　　　　　
  Koki Yuasa; Tomoyuki Shikata; Takayoshi Ichikawa; Yu Tamura; Yoshitaka Nishiyama
  Harmful Algae, Volume：99, First page：101938, Last page：101938, Nov. 2020, [Reviewed], [Corresponding], ［International magazine］
  The raphidophyte Chattonella antiqua is a single-celled alga that forms 'red tides' in coastal areas. C. antiqua produces superoxide anions (O2-), the excessive production of which has been associated with fish mortality. It is suggested that putative NADPH oxidase in the outer membrane oxidizes intracellular NADPH to produce O2- and secrete it externally. Earlier studies revealed that photosynthetic electron transport, a major producer of NADPH in photosynthetic organisms, is involved in the production of O2- in C. antiqua but the details of the O2- production mechanism have yet to be elucidated. Since nutrient deficiency adversely affects the formation of blooms of C. antiqua, in this study, we examined the effects of nutrient deficiency on O2- production in C. antiqua. When cells were grown under nitrogen (N)- or phosphorus (P)-deficient conditions, the production of O2- was stimulated. In particular, the extracellular levels of O2- under N- or P-deficient conditions were high during the dark period when photosynthetic activities in terms of actual quantum efficiency and photochemical quenching were low. The extracellular levels of O2- under the nutrient-deficient conditions were unaffected by the presence of 3-(3,4-dichlorophenyl)-1,1‑dimethylurea (DCMU), an inhibitor of photosynthetic electron transport, but decreased when the nutrients were present. Furthermore, the intracellular ratio of NADPH to NADP+ under N- or P-deficient conditions was higher than that under nutrient-replete conditions. These observations suggest that another metabolic pathway, independent of photosynthesis, provides NADPH for the production of O2- under nutrient deficiency.
  Elsevier BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.hal.2020.101938
  DOI ID：10.1016/j.hal.2020.101938, ISSN：1568-9883, PubMed ID：33218451
• Long-Chain Saturated Fatty Acids, Palmitic and Stearic Acids, Enhance the Repair of Photosystem II
  Haruhiko Jimbo; Kensuke Takagi; Takashi Hirashima; Yoshitaka Nishiyama; Hajime Wada
  International Journal of Molecular Sciences, Volume：21, Number：20, First page：7509, Last page：7509, Oct. 2020, [Reviewed]
  Free fatty acids (FFA) generated in cyanobacterial cells can be utilized for the biodiesel that is required for our sustainable future. The combination of FFA and strong light induces severe photoinhibition of photosystem II (PSII), which suppresses the production of FFA in cyanobacterial cells. In the present study, we examined the effects of exogenously added FFA on the photoinhibition of PSII in Synechocystis sp. PCC 6803. The addition of lauric acid (12:0) to cells accelerated the photoinhibition of PSII by inhibiting the repair of PSII and the de novo synthesis of D1. α-Linolenic acid (18:3) affected both the repair of and photodamage to PSII. Surprisingly, palmitic (16:0) and stearic acids (18:0) enhanced the repair of PSII by accelerating the de novo synthesis of D1 with the mitigation of the photoinhibition of PSII. Our results show chemical potential of FFA in the regulation of PSII without genetic manipulation.
  MDPI AG, Scientific journal
  DOI：https://doi.org/10.3390/ijms21207509
  DOI ID：10.3390/ijms21207509, eISSN：1422-0067
• Vertical distribution of a harmful red-tide dinoflagellate, Karenia mikimotoi, at the decline stage of blooms　　　　　　　　　　　　　　　
  Tomoyuki Shikata; Saho Kitatsuji; Kazuo Abe; Goh Onitsuka; Tadashi Matsubara; Natsuko Nakayama; Koki Yuasa; Yoshitaka Nishiyama; Ken-Ichiro Mizuno; Takeshi Masuda; Kiyohito Nagai
  Journal of Sea Research, Volume：165, First page：101960, Last page：101960, Oct. 2020, [Reviewed]
  The red-tide dinoflagellate Karenia mikimotoi can vertically migrate similar to 20 m in a day. This property enables K. mikimotoi to acquire nutrients over a wide range of depths and to receive optimal irradiance. We conducted day and night observations of diurnal vertical migrations (DVMs) during the declining stage of blooms and daily-weekly investigations of the relationship between environmental factors and a K. mikimotoi bloom in four different bays of western Japan. Moreover, we performed correlation analysis between DVM parameters, such as migratory distance and environmental conditions, using data from the present study and previous studies, which DVMs were observed at the developmental or stationary stage of K. mikimotoi bloom. Observations of evident DVMs of K. mikimotoi were commonly absent, although the depths where K. mikimotoi accumulated throughout the day differed among observations. Migratory distance showed a positive correlation with the number of days it took for the bloom to decline and a negative correlation with the vertical stratification. Precipitation was low, irradiance was high, and dissolved inorganic nitrogen (DIN) and phosphorus (DIP) concentrations were inadequate for cell growth 1-2 weeks before the DVM observations. Moreover, average DIP concentration at the depth of the highest K. mikimotoi cell concentration in the water column and the growth rate estimated from DIN and DIP concentrations during the DVM observations showed positive correlations with migratory distance. During DVM observation, the amount of light received was inadequate for growth when K. mikimotoi cells remained in deep waters, and photoinhibition occurred when they remained in surface waters. The results suggest that adverse conditions, such as nutrient deficiency and strong stratification, may prevent K. mikimotoi from achieving the benefits of DVM behavior and thereby promote the collapse of a bloom.
  Elsevier BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.seares.2020.101960
  DOI ID：10.1016/j.seares.2020.101960, ISSN：1385-1101, eISSN：1873-1414, Web of Science ID：WOS:000582501900007
• Elevated Levels of Specific Carotenoids During Acclimation to Strong Light Protect the Repair of Photosystem II in Synechocystis sp. PCC 6803
  Taichi Izuhara; Ikumi Kaihatsu; Haruhiko Jimbo; Shinichi Takaichi; Yoshitaka Nishiyama
  Frontiers in Plant Science, Volume：11, Jul. 2020, [Reviewed], [Corresponding]
  Frontiers Media SA, Scientific journal
  DOI：https://doi.org/10.3389/fpls.2020.01030
  DOI ID：10.3389/fpls.2020.01030, eISSN：1664-462X
• Resilience under climate change
  Yoshitaka Nishiyama
  Nature Plants, Volume：6, Number：5, First page：442, Last page：443, May 2020, [Reviewed], [Lead, Corresponding]
  Springer Science and Business Media LLC, Scientific journal
  DOI：https://doi.org/10.1038/s41477-020-0639-x
  DOI ID：10.1038/s41477-020-0639-x, eISSN：2055-0278
• Extracellular secretion of superoxide is regulated by photosynthetic electron transport in the noxious red-tide-forming raphidophyte Chattonella antiqua　　　　　　　　　　　　　　　
  Koki Yuasa; Tomoyuki Shikata; Saho Kitatsuji; Yasuhiro Yamasaki; Yoshitaka Nishiyama
  Journal of Photochemistry and Photobiology B: Biology, Volume：205, First page：111839, Last page：111839, Apr. 2020, [Reviewed], [Corresponding], ［International magazine］
  The raphidophyte Chattonella antiqua is a noxious red-tide-forming alga that harms fish culture and the aquatic environment. Chattonella antiqua produces and secretes superoxide anions (O2-), and excessive secretion of O2- into the water has been associated with fish mortality. It is known that strong light stimulates the production of O2- in Chattonella spp. but the mechanism of the light-induced production of O2- remains to be clarified. In the present study, we examined the effects of light on extracellular levels of O2- and photosynthesis in C. antiqua. Extracellular levels of O2- rose during growth under high-intensity light, and the level of O2- was correlated with the photosynthetic parameter qP, which reflects the rate of transport of electrons downstream of photosystem II. The production of O2- was inhibited in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea, an inhibitor of photosynthetic electron transport, suggesting that reducing power derived from electron transport might be required for the production of O2-. By contrast, the production of O2- was enhanced in the presence of glycolaldehyde, an inhibitor of the Calvin-Benson cycle, suggesting that the accumulation of NADPH might stimulate the production of O2-. Thus, it is likely that the production of O2- is regulated by photosynthesis in C. antiqua.
  Elsevier BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.jphotobiol.2020.111839
  DOI ID：10.1016/j.jphotobiol.2020.111839, ISSN：1011-1344, PubMed ID：32146272
• Light-inducible expression of translation factor EF-Tu during acclimation to strong light enhances the repair of photosystem II.　　　　　　　　　　　　　　　
  Jimbo H; Izuhara T; Hihara Y; Hisabori T; Nishiyama Y
  Proceedings of the National Academy of Sciences of the United States of America, Volume：116, Number：42, First page：21268, Last page：21273, Oct. 2019, [Reviewed]
  DOI：https://doi.org/10.1073/pnas.1909520116
  DOI ID：10.1073/pnas.1909520116, ISSN：0027-8424, PubMed ID：31570574
• RNA-Seq Analysis Reveals Genes Related to Photoreception, Nutrient Uptake, and Toxicity in a Noxious Red-Tide Raphidophyte Chattonella antiqua.　　　　　　　　　　　　　　　
  Shikata T; Takahashi F; Nishide H; Shigenobu S; Kamei Y; Sakamoto S; Yuasa K; Nishiyama Y; Yamasaki Y; Uchiyama I
  Frontiers in Microbiology, Volume：10, First page：1764, Last page：1764, 2019, [Reviewed], ［International magazine］
  Aquaculture industries are under threat from noxious red tides, but harm can be mitigated by precautions such as early harvesting and restricting fish feeding to just before the outbreak of a red tide. Therefore, accurate techniques for forecasting red-tide outbreaks are strongly needed. Omics analyses have the potential to expand our understanding of the eco-physiology of these organisms at the molecular level, and to facilitate identification of molecular markers for forecasting their population dynamics and occurrence of damages to fisheries. Red tides of marine raphidophytes, especially Chattonella species, often extensively harm aquaculture industries in regions with a temperate climate around the world. A red tide of Chattonella tends to develop just after an input of nutrients along the coast. Chattonella displays diurnal vertical migration regulated by a weak blue light, so it photosynthesizes in the surface layer during the daytime and takes up nutrients in the bottom layer during the nighttime. Superoxide produced by Chattonella cells is a strong candidate for the cause of its toxicity to bacteria and fishes. Here we conducted mRNA-seq of Chattonella antiqua to identify genes with functions closely related to the dynamics of the noxious red tide, such as photosynthesis, photoreception, nutrient uptake, and superoxide production. The genes related to photosynthetic pigment biosynthesis and nutrient uptake had high similarity with those of model organisms of plants and algae and other red-tide microalgae. We identified orthologous genes of photoreceptors such as aureochrome (newly five genes), the cryptochrome/photolyase (CRY/PHR) family (6-4PHR, plant CRY or cyclobutane pyrimidine dimer [CPD] Class III, CPD Class II, and CRY-DASH), and phytochrome (four genes), which regulate various physiological processes such as flagellar motion and cell cycle in model organisms. Six orthologous genes of NADPH oxidase, which produces superoxide on the cell membrane, were found and divided into two types: one with 5-6 transmembrane domains and another with 11 transmembrane domains. The present study should open the way for analyzing the eco-physiological features of marine raphidophytes at the molecular level.
  English, Scientific journal
  DOI：https://doi.org/10.3389/fmicb.2019.01764
  DOI ID：10.3389/fmicb.2019.01764, PubMed ID：31417538, PubMed Central ID：PMC6685483
• Overexpression of orange carotenoid protein protects the repair of photosystem II under strong light in Synechocystis sp. PCC 6803.　　　　　　　　　　　　　　　
  Takahashi H; Kusama Y; Li X; Takaichi S; Nishiyama Y
  Plant & Cell Physiology, Volume：60, Number：2, First page：367, Last page：375, Nov. 2018, [Reviewed]
  Orange carotenoid protein (OCP) plays a vital role in the thermal dissipation of excitation energy in the photosynthetic machinery of the cyanobacterium Synechocystis sp. PCC 6803. To clarify the role of OCP in the protection of PSII from strong light, we generated an OCP-overexpressing strain of Synechocystis and examined the effects of overexpression on the photoinhibition of PSII. In OCP-overexpressing cells, thermal dissipation of energy was enhanced and the extent of photoinhibition of PSII was reduced. However, photodamage to PSII, as monitored in the presence of lincomycin, was unaffected, suggesting that overexpressed OCP protects the repair of PSII. Furthermore, the synthesis de novo of proteins in thylakoid membranes, such as the D1 protein which is required for the repair of PSII, was enhanced in OCP-overexpressing cells under strong light, while the production of singlet oxygen was suppressed. Thus, the enhanced thermal dissipation of energy via overexpressed OCP might support the repair of PSII by protecting protein synthesis from oxidative damage by singlet oxygen under strong light, with the resultant mitigation of photoinhibition of PSII.
  OXFORD UNIV PRESS, English, Scientific journal
  DOI：https://doi.org/10.1093/pcp/pcy218
  DOI ID：10.1093/pcp/pcy218, ISSN：0032-0781, eISSN：1471-9053, PubMed ID：30398652, Web of Science ID：WOS:000459634300010
• Adverse effects of strong light and nitrogen deficiency cell viability, photosynthesis, and motility of the red-tide dinoflagellate Karenia mikimotoi.　　　　　　　　　　　　　　　
  Yuasa K; Shikata T; Kuwahara Y; Nishiyama Y
  Phycologia, Volume：57, Number：5, First page：525, Last page：533, Jul. 2018, [Reviewed]
  The dinoflagellate Karenia mikimotoi is a red tide-forming alga that causes serious damage to aquaculture in coastal areas around the world. Its eco-physiological characteristics have been investigated extensively but conditions associated with declines of red tides of K. mikimotoi remain unknown. In the present study, we investigated the effects of light and nutrients on the viability, activity of photosystem II (PSII), and motility of K. mikimotoi. Cells were incubated under low (100 mu mol photons m(-2) s(-1) on a 12:12 light: dark cycle of illumination) or high irradiance (1000 mu mol photons m(-2) s(-1)) for 4 h in the middle of the photoperiod, in different media. Under low light, most cells survived for about 1 month in media depleted of nitrogen (N) and phosphorus (P), similar to their survival pattern in complete medium. However, when cells that had been pre-incubated in N-depleted medium for 7 d were incubated under high light in an N-depleted medium, cell density and PSII activity declined within a few days. In P-depleted and complete media, there were no significant differences in cell density and PSII activity between low and high light, at least for 10 d. Furthermore, PSII activity was much more sensitive to photoinhibition in N-depleted than in complete medium. The rhythm of diurnal vertical migration of K. mikimotoi was observed in very low light (10 mu mol photons m(-2) s(-1)) in different media. The rhythm became obscure in N- and P-depleted media; in fact, most cells stayed in the surface layer all day in N-depleted medium. Moreover, cells accumulating in surface layers in N- and P-depleted media descended very little, even when irradiated with high light. These observations suggest that N-deficiency might trap cells in the surface layer and increase their susceptibility to photoinhibition of PSII, possibly leading to cell death. The combination of N-deficiency and high light thus appears to be an important factor that determines the decline of red tides of K. mikimotoi.
  ALLEN PRESS INC, English, Scientific journal
  DOI：https://doi.org/10.2216/17-61.1
  DOI ID：10.2216/17-61.1, ISSN：0031-8884, Web of Science ID：WOS:000445100400004
• Interaction of the GntR-family transcription factor Sll1961 with thioredoxin in the cyanobacterium Synechocystis sp. PCC 6803.　　　　　　　　　　　　　　　
  Junichi Kujirai; Sato Nanba; Taro Kadowaki; Yoshiki Oka; Yoshitaka Nishiyama; Yuuki Hayashi; Munehito Arai; Yukako Hihara
  Scientific reports, Volume：8, Number：1, First page：6666, Last page：6666, Apr. 2018, [Reviewed], ［International magazine］
  Changes in the redox state of the photosynthetic electron transport chain act as a signal to trigger acclimation responses to environmental cues and thioredoxin has been suggested to work as a key factor connecting the redox change with transcriptional regulation in the cyanobacterium Synechocystis sp. PCC 6803. We screened for redox-dependent transcription factors interacting with thioredoxin M (TrxM) and isolated the GntR-type transcription factor Sll1961 previously reported to be involved in acclimation responses of the photosynthetic machinery. Biochemical analyses using recombinant Sll1961 proteins of wild type and mutants of three cysteine residues, C124, C229 and C307, revealed that an intramolecular disulfide bond is formed between C229 and C307 under oxidizing conditions and TrxM can reduce it by attacking C307. Sll1961 exists in a dimeric form of about 80 kDa both under reducing and oxidizing conditions. C124 can form an intermolecular disulfide bond but it is not essential for dimerization. Based on these observations, tertiary structure models of the Sll1961 homodimer and the Sll1961-TrxM complex were constructed.
  English, Scientific journal
  DOI：https://doi.org/10.1038/s41598-018-25077-5
  DOI ID：10.1038/s41598-018-25077-5, PubMed ID：29703909, PubMed Central ID：PMC5923263
• Oxidation of translation factor EF-Tu inhibits the repair of photosystem II　　　　　　　　　　　　　　　
  Haruhiko Jimbo; Rayakorn Yutthanasirikul; Takanori Nagano; Toru Hisabori; Yukako Hihara; Yoshitaka Nishiyama
  Plant Physiology, Volume：176, Number：4, First page：2691, Last page：2699, Apr. 2018, [Reviewed]
  The repair of photosystem II (PSII) is particularly sensitive to oxidative stress and the inhibition of repair is associated with oxidative damage to the translational elongation system in the cyanobacterium Synechocystis sp. PCC 6803. However, the molecular mechanisms underlying this inhibition are unknown. We previously demonstrated in vitro that EF-Tu, a translation factor that delivers aminoacyl-tRNA to the ribosome, is inactivated by reactive oxygen species via oxidation of the Cys residue Cys-82. In this study, we examined the physiological role of the oxidation of EF-Tu in Synechocystis. Under strong light, EF-Tu was rapidly oxidized to yield oxidized monomers in vivo. We generated a Synechocystis transformant that expressed mutated EF-Tu in which Cys-82 had been replaced with a Ser residue. Under strong light, the de novo synthesis of proteins that are required for PSII repair, such as D1, was enhanced in the transformant and photoinhibition of PSII was alleviated. However, photodamage to PSII, measured in the presence of lincomycin, was similar between the transformant and wild-type cells, suggesting that expression of mutated EF-Tu might enhance the repair of PSII. Alleviating photoinhibition through mutation of EF-Tu did not alter cell growth under strong light, perhaps due to the enhanced production of reactive oxygen species. These observations suggest that the oxidation of EF-Tu under strong light inhibits PSII repair, resulting in the stimulation of photoinhibition.
  American Society of Plant Biologists, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.18.00037
  DOI ID：10.1104/pp.18.00037, ISSN：1532-2548, PubMed ID：29439212, SCOPUS ID：85045519528
• ATP is a driving force in the repair of photosystem II during photoinhibition　　　　　　　　　　　　　　　
  Norio Murata; Yoshitaka Nishiyama
  Plant Cell and Environment, Volume：41, Number：2, First page：285, Last page：299, Feb. 2018, [Reviewed]
  Repair of photosystem II (PSII) during photoinhibition involves replacement of photodamaged D1 protein by newly synthesized D1 protein. In this review, we summarize evidence for the indispensability of ATP in the degradation and synthesis of D1 during the repair of PSII. Synthesis of one molecule of the D1 protein consumes more than 1,300 molecules of ATP equivalents. The degradation of photodamaged D1 by FtsH protease also consumes approximately 240 molecules of ATP. In addition, ATP is required for several other aspects of the repair of PSII, such as transcription of psbA genes. These requirements for ATP during the repair of PSII have been demonstrated by experiments showing that the synthesis of D1 and the repair of PSII are interrupted by inhibitors of ATP synthase and uncouplers of ATP synthesis, as well as by mutation of components of ATP synthase. We discuss the contribution of cyclic electron transport around photosystem I to the repair of PSII. Furthermore, we introduce new terms relevant to the regulation of the PSII repair, namely, “ATP-dependent regulation” and “redox-dependent regulation,” and we discuss the possible contribution of the ATP-dependent regulation of PSII repair under environmental stress.
  Blackwell Publishing Ltd, English
  DOI：https://doi.org/10.1111/pce.13108
  DOI ID：10.1111/pce.13108, ISSN：1365-3040, PubMed ID：29210214, SCOPUS ID：85039163429
• The LexA transcription factor regulates fatty acid biosynthetic genes in the cyanobacterium Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Ayumi Kizawa; Akihito Kawahara; Kosuke Takashima; Yasushi Takimura; Yoshitaka Nishiyama; Yukako Hihara
  PLANT JOURNAL, Volume：92, Number：2, First page：189, Last page：198, Oct. 2017, [Reviewed]
  Specific transcription factors have been identified in various heterotrophic bacterial species that regulate the sets of genes required for fatty acid metabolism. Here, we report that expression of the fab genes, encoding fatty acid biosynthetic enzymes, is regulated by the global regulator LexA in the photoautotrophic cyanobacterium Synechocystis sp. PCC 6803. Sll1626, an ortholog of the well-known LexA repressor involved in the SOS response in heterotrophic bacteria, was isolated from crude extracts of Synechocystis by DNA affinity chromatography, reflecting its binding to the upstream region of the acpP-fabF and fabI genes. An electrophoresis mobility shift assay revealed that the recombinant LexA protein can bind to the upstream region of each fab gene tested (fabD, fabH, fabF, fabG, fabZ and fabI). Quantitative RT-PCR analysis of the wild type and a lexA-disrupted mutant strain suggested that LexA acts as a repressor of the fab genes involved in initiation of fatty acid biosynthesis (fabD, fabH and fabF) and the first reductive step in the subsequent elongation cycle (fabG) under normal growth conditions. Under nitrogen-depleted conditions, downregulation of fab gene expression is partly achieved through an increase in LexA-repressing activity. In contrast, under phosphate-depleted conditions, fab gene expression is upregulated, probably due to the loss of repression by LexA. We further demonstrate that elimination of LexA largely increases the production of fatty acids in strains modified to secrete free fatty acids.
  WILEY, English, Scientific journal
  DOI：https://doi.org/10.1111/tpj.13644
  DOI ID：10.1111/tpj.13644, ISSN：0960-7412, eISSN：1365-313X, PubMed ID：28744961, Web of Science ID：WOS:000412680200004
• Disturbance of cell-size determination by forced overproduction of sulfoquinovosyl diacylglycerol in the cyanobacterium Synechococcus elongatus PCC 7942　　　　　　　　　　　　　　　
  Norihiro Sato; Yuki Ebiya; Ryutaro Kobayashi; Yoshitaka Nishiyama; Mikio Tsuzuki
  BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Volume：487, Number：3, First page：734, Last page：739, Jun. 2017, [Reviewed]
  Sulfoquinovosyl diacylglycerol (SQDG) is present in the membranes of cyanobacteria or their descendants, plastids at species-dependent levels. We investigated the physiological significance of the intrinsic SQDG content in the cyanobacterium Synechococcus elongatus PCC 7942, with the use of its mutant, in which the genes for SQDG synthesis, sqdB and sqdX, were overexpressed. The mutant showed a 1.3-fold higher content of SQDG (23.6 mol% relative to total cellular lipids, cf., 17.1 mol% in the control strain) with much less remarkable effects on the other lipid classes. Simultaneously observed were 1.6-to 1.9-fold enhanced mRNA levels for the genes responsible for the synthesis of the lipids other than SQDG, as if to compensate for the SQDG overproduction. Meanwhile, the mutant showed no injury to cell growth, however, cell length was increased (6.1 +/- 23, cf., 3.8 +/- 0.8 mu m in the control strain). Accordingly with this, a wide range of genes responsible for cell division were 1.6-2.4-fold more highly expressed in the mutant. These results suggested that a regulatory mechanism for lipid homeostasis functions in the mutant, and that SQDG has to be kept from surpassing the intrinsic content in S. elongatus for repression of the abnormal expression of cell division-related genes and, inevitably, for normal cell division. (C) 2017 Elsevier Inc. All rights reserved.
  ACADEMIC PRESS INC ELSEVIER SCIENCE, English, Scientific journal
  DOI：https://doi.org/10.1016/j.bbrc.2017.04.129
  DOI ID：10.1016/j.bbrc.2017.04.129, ISSN：0006-291X, eISSN：1090-2104, PubMed ID：28450108, Web of Science ID：WOS:000401783400039
• Moderate Heat Stress Stimulates Repair of Photosystem II During Photoinhibition in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Mamoru Ueno; Penporn Sae-Tang; Yuri Kusama; Yukako Hihara; Mami Matsuda; Tomohisa Hasunuma; Yoshitaka Nishiyama
  PLANT AND CELL PHYSIOLOGY, Volume：57, Number：11, First page：2417, Last page：2426, Nov. 2016, [Reviewed]
  Examination of the effects of high temperature on the photoinhibition of photosystem II (PSII) in the cyanobacterium Synechocystis sp. PCC 6803 revealed that the extent of photoinhibition of PSII was lower at moderately high temperatures (35-42 degrees C) than at 30 degrees C. Photodamage to PSII, as determined in the presence of chloramphenicol, which blocks the repair of PSII, was accelerated at the moderately high temperatures but the effects of repair were greater than those of photodamage. The synthesis de novo of the D1 protein, which is essential for the repair of PSII, was enhanced at 38 degrees C. Electron transport and the synthesis of ATP were also enhanced at 38 degrees C, while levels of reactive oxygen species fell. Inhibition of the Calvin-Benson cycle with glycolaldehyde abolished the enhancement of repair of PSII at 38 degrees C, suggesting that an increase in the activity of the Calvin-Benson cycle might be required for the enhancement of repair at moderately high temperatures. The synthesis de novo of metabolic intermediates of the Calvin-Benson cycle, such as 3-phosphoglycerate, was also enhanced at 38 degrees C. We propose that moderate heat stress might enhance the repair of PSII by stimulating the synthesis of ATP and depressing the production of reactive oxygen species, via the stimulation of electron transport and suppression of the accumulation of excess electrons on the acceptor side of photosystem I, which might be driven by an increase in the activity of the Calvin-Benson cycle.
  OXFORD UNIV PRESS, English, Scientific journal
  DOI：https://doi.org/10.1093/pcp/pcw153
  DOI ID：10.1093/pcp/pcw153, ISSN：0032-0781, eISSN：1471-9053, PubMed ID：27565206, Web of Science ID：WOS:000393158000016
• Overexpressed Superoxide Dismutase and Catalase Act Synergistically to Protect the Repair of PSII during Photoinhibition in Synechococcus elongatus PCC 7942　　　　　　　　　　　　　　　
  Penporn Sae-Tang; Yukako Hihara; Isao Yumoto; Yoshitake Orikasa; Hidetoshi Okuyama; Yoshitaka Nishiyama
  PLANT AND CELL PHYSIOLOGY, Volume：57, Number：9, First page：1899, Last page：1907, Sep. 2016, [Reviewed]
  The repair of PSII under strong light is particularly sensitive to reactive oxygen species (ROS), such as the superoxide radical and hydrogen peroxide, and these ROS are efficiently scavenged by superoxide dismutase (SOD) and catalase. In the present study, we generated transformants of the cyanobacterium Synechococcus elongatus PCC 7942 that overexpressed an iron superoxide dismutase (Fe-SOD) from Synechocystis sp. PCC 6803; a highly active catalase (VktA) from Vibrio rumoiensis; and both enzymes together. Then we examined the sensitivity of PSII to photoinhibition in the three strains. In cells that overexpressed either Fe-SOD or VktA, PSII was more tolerant to strong light than it was in wild-type cells. Moreover, in cells that overexpressed both Fe-SOD and VktA, PSII was even more tolerant to strong light. However, the rate of photodamage to PSII, as monitored in the presence of chloramphenicol, was similar in all three transformant strains and in wild-type cells, suggesting that the overexpression of these ROS-scavenging enzymes might not protect PSII from photodamage but might protect the repair of PSII. Under strong light, intracellular levels of ROS fell significantly, and the synthesis de novo of proteins that are required for the repair of PSII, such as the D1 protein, was enhanced. Our observations suggest that overexpressed Fe-SOD and VktA might act synergistically to alleviate the photoinhibition of PSII by reducing intracellular levels of ROS, with resultant protection of the repair of PSII from oxidative inhibition.
  OXFORD UNIV PRESS, English, Scientific journal
  DOI：https://doi.org/10.1093/pcp/pcw110
  DOI ID：10.1093/pcp/pcw110, ISSN：0032-0781, eISSN：1471-9053, PubMed ID：27328698, Web of Science ID：WOS:000384717400009
• Light spectrum regulates cell accumulation during daytime in the raphidophyte Chattonella antiqua causing noxious red tides　　　　　　　　　　　　　　　
  Tomoyuki Shikata; Shigeru Matsunaga; Yusuke Kuwahara; Sho Iwahori; Yoshitaka Nishiyama
  JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY, Volume：160, First page：128, Last page：133, Jul. 2016, [Reviewed]
  Most marine raphidophyte species cause noxious red tides in temperate coastal areas around the world. It is known that swimming abilities enable raphidophytes to accumulation of cells and to actively acquire light at surface layers and nutrients over a wide depth range. However, it remains unclear how the swimming behavior is affected by environmental conditions, especially light condition. In the present study, we observed the accumulation of the harmful red-tide raphidophyte Chattonella antiqua under various light conditions during the daytime in the laboratory. When exposed to ultraviolet-A/blue light (320-480 nm) or red light (640-680 nm) from above, cells moved downward. In the case of blue light (455 nm), cells started to swim downward after 5-15 min of irradiation at a photon flux density >= 10 mu mol m(-2) s(-1). When exposed to monochromatic lights (400-680 nm) from the side, cells moved away from the blue light source and then descended, but just moved downward under red light. However, mixing of green/orange light (520-630 nm) diminished the effects of blue light. When exposed to a mixture of 30 mu mol m(-2) s(-1) of blue light (440 nm) and >= 6 mu mol m(-2) s(-1) of yellow light (560 nm) from above, cells did not move downward. These results indicate that blue light induces negative phototaxis and ultraviolet-A/blue and red lights induce descending, and green/orange light cancels out their effects in C antiqua. (C) 2016 Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE SA, English, Scientific journal
  DOI：https://doi.org/10.1016/j.jphotobiol.2016.03.046
  DOI ID：10.1016/j.jphotobiol.2016.03.046, ISSN：1011-1344, PubMed ID：27107332, Web of Science ID：WOS:000378453500016
• A Feed-Forward Loop Consisting of the Response Regulator RpaB and the Small RNA PsrR1 Controls Light Acclimation of Photosystem I Gene Expression in the Cyanobacterium Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Taro Kadowaki; Ryuta Nagayama; Jens Georg; Yoshitaka Nishiyama; Annegret Wilde; Wolfgang R. Hess; Yukako Hihara
  PLANT AND CELL PHYSIOLOGY, Volume：57, Number：4, First page：813, Last page：823, Apr. 2016, [Reviewed]
  Since cyanobacteria need to decrease PSI content to avoid absorption of excess light energy, down-regulation of PSI gene expression is one of the key characteristics of the high-light (HL) acclimation response. The transcriptional regulator RpaB and the small RNA PsrR1 (photosynthesis regulatory RNA1) have been suggested to be the two most critical factors for this response in Synechocystis sp. PCC 6803. In this study, we found that the HLR1 DNA-binding motif, the recognition sequence for RpaB, is highly conserved in the core promoter region of the psrR1 gene among cyanobacterial species. Gel mobility shift assay revealed that RpaB binds to the HLR1 sequence of psrR1 in vitro. RNA gel blot analysis together with chromatin affinity purification (ChAP) analysis suggested that PSI genes are activated and the psrR1 gene is repressed by the binding of RpaB under low-light (LL) conditions. A decrease in DNA binding affinity of RpaB occurs within 5 min after the shift from LL to HL conditions, leading to the prompt decrease in PSI promoter activity together with derepression of psrR1 gene expression. Accumulating PsrR1 molecules then prevent translation from pre-existing PSI transcripts. By this dual repression at transcriptional and post-transcriptional levels, rapid and strict down-regulation of PSI expression under HL is secured. Our findings suggest that RpaB and PsrR1 constitute a feed-forward loop for the regulation of PSI gene expression to achieve a rapid acclimation response to the damaging HL conditions.
  OXFORD UNIV PRESS, English, Scientific journal
  DOI：https://doi.org/10.1093/pcp/pcw028
  DOI ID：10.1093/pcp/pcw028, ISSN：0032-0781, eISSN：1471-9053, PubMed ID：26872833, Web of Science ID：WOS:000376654100015
• Oxidation of a Cysteine Residue in Elongation Factor EF-Tu Reversibly Inhibits Translation in the Cyanobacterium Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Rayakorn Yutthanasirikul; Takanori Nagano; Haruhiko Jimbo; Yukako Hihara; Takashi Kanamori; Takuya Ueda; Takamitsu Haruyama; Hiroki Konno; Keisuke Yoshida; Toru Hisabori; Yoshitaka Nishiyama
  JOURNAL OF BIOLOGICAL CHEMISTRY, Volume：291, Number：11, First page：5860, Last page：5870, Mar. 2016, [Reviewed]
  Translational elongation is susceptible to inactivation by reactive oxygen species (ROS) in the cyanobacterium Synechocystis sp. PCC 6803, and elongation factor G has been identified as a target of oxidation by ROS. In the present study we examined the sensitivity to oxidation by ROS of another elongation factor, EF-Tu. The structure of EF-Tu changes dramatically depending on the bound nucleotide. Therefore, we investigated the sensitivity to oxidation in vitro of GTP- and GDP-bound EF-Tu as well as that of nucleotide-free EF-Tu. Assays of translational activity with a reconstituted translation system from Escherichia coli revealed that GTP-bound and nucleotide-free EF-Tu were sensitive to oxidation by H2O2, whereas GDP-bound EF-Tu was resistant to H2O2. The inactivation of EF-Tu was the result of oxidation of Cys-82, a single cysteine residue, and subsequent formation of both an intermolecular disulfide bond and sulfenic acid. Replacement of Cys-82 with serine rendered EF-Tu resistant to inactivation by H2O2, confirming that Cys-82 was a target of oxidation. Furthermore, oxidized EF-Tu was reduced and reactivated by thioredoxin. Gel-filtration chromatography revealed that some of the oxidized nucleotide-free EF-Tu formed large complexes of >30 molecules. Atomic force microscopy revealed that such large complexes dissociated into several smaller aggregates upon the addition of dithiothreitol. Immunological analysis of the redox state of EF-Tu in vivo showed that levels of oxidized EF-Tu increased under strong light. Thus, resembling elongation factor G, EF-Tu appears to be sensitive to ROS via oxidation of a cysteine residue, and its inactivation might be reversed in a redox-dependent manner.
  AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, English, Scientific journal
  DOI：https://doi.org/10.1074/jbc.M115.706424
  DOI ID：10.1074/jbc.M115.706424, ISSN：0021-9258, eISSN：1083-351X, PubMed ID：26786107, Web of Science ID：WOS:000372551800032
• RNA-seq Profiling Reveals Novel Target Genes of LexA in the Cyanobacterium Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Ayumi Kizawa; Akihito Kawahara; Yasushi Takimura; Yoshitaka Nishiyama; Yukako Hihara
  FRONTIERS IN MICROBIOLOGY, Volume：7, First page：193, Feb. 2016, [Reviewed]
  LexA is a well-established transcriptional repressor of SOS genes induced by DNA damage in Escherichia coil and other bacterial species. However, LexA in the cyanobacterium Synechocystis sp. PCC 6803 has been suggested not to be involved in SOS response. In this study, we performed RNA-seq analysis of the wild-type strain and the lexA-disrupted mutant to obtain the comprehensive view of LexA-regulated genes in Synechocystis. Disruption of lexA positively or negatively affected expression of genes related to various cellular functions such as phototactic motility, accumulation of the major compatible solute glucosylglycerol and subunits of bidirectional hydrogenase, photosystem I, and phycobilisome complexes. We also observed increase in the expression level of genes related to iron and manganese uptake in the mutant at the later stage of cultivation. However, none of the genes related to DNA metabolism were affected by disruption of lexA. DNA gel mobility shift assay using the recombinant LexA protein suggested that LexA binds to the upstream region of pilA7, pilA9, ggpS. and slr1670 to directly regulate their expression, but changes in the expression level of photosystem I genes by disruption of lexA is likely a secondary effect.
  FRONTIERS MEDIA SA, English, Scientific journal
  DOI：https://doi.org/10.3389/fmicb.2016.00193
  DOI ID：10.3389/fmicb.2016.00193, ISSN：1664-302X, PubMed ID：26925056, Web of Science ID：WOS:000370563900001
• Rapid acquisition of high-affinity DNA aptamer motifs recognizing microbial cell surfaces using polymer-enhanced capillary transient isotachophoresis　　　　　　　　　　　　　　　
  Shingo Saito; Kazuki Hirose; Maho Tsuchida; Koji Wakui; Keitaro Yoshimoto; Yoshitaka Nishiyama; Masami Shibukawa
  CHEMICAL COMMUNICATIONS, Volume：52, Number：3, First page：461, Last page：464, 2016, [Reviewed]
  We present a polymer-enhanced capillary transient isotachophoresis (PectI) selection methodology for acquisition of high-affinity (kinetically inert) DNA aptamers capable of recognizing distinct microbial cell surfaces, which requires only a single electrophoretic separation between particles (free cells and cells bound with aptamers) and molecules (unbound or dissociated DNA) in free solution.
  ROYAL SOC CHEMISTRY, English, Scientific journal
  DOI：https://doi.org/10.1039/c5cc07268a
  DOI ID：10.1039/c5cc07268a, ISSN：1359-7345, eISSN：1364-548X, PubMed ID：26525483, Web of Science ID：WOS:000367259200005
• Analysis of spontaneous suppressor mutants from the photomixotrophically grown pmgA-disrupted mutant in the cyanobacterium Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Yoshiki Nishijima; Yu Kanesaki; Hirofumi Yoshikawa; Takako Ogawa; Kintake Sonoike; Yoshitaka Nishiyama; Yukako Hihara
  PHOTOSYNTHESIS RESEARCH, Volume：126, Number：2-3, First page：465, Last page：475, Dec. 2015, [Reviewed]
  The pmgA-disrupted (Delta pmgA) mutant in the cyanobacterium Synechocystis sp. PCC 6803 suffers severe growth inhibition under photomixotrophic conditions. In order to elucidate the key factors enabling the cells to grow under photomixotrophic conditions, we isolated spontaneous suppressor mutants from the Delta pmgA mutant derived from a single colony. When the Delta pmgA mutant was spread on a BG11 agar plate supplemented with glucose, colonies of suppressor mutants appeared after the bleaching of the background cells. We identified the mutation site of these suppressor mutants and found that 11 mutants out of 13 had a mutation in genes related to the type 1 NAD(P)H dehydrogenase (NDH-1) complex. Among them, eight mutants had mutations within the ndhF3 (sll1732) gene: R32stop, W62stop, V147I, G266V, G354W, G586C, and deletion of 7 bp within the coding region. One mutant had one base insertion in the putative -10 box of the ndhC (slr1279) gene, leading to the decrease in the transcripts of the ndhCKJ operon. Two mutants had one base insertion and deletion in the coding region of cupA (sll1734), which is co-transcribed with ndhF3 and ndhD3 and comprises together a form of NDH-1 complex (NDH-1MS complex) involved in inducible high-affinity CO2 uptake. The results indicate that the loss of the activity of this complex effectively rescues the Delta pmgA mutant under photomixotrophic condition with 1 % CO2. However, little difference among WT and mutants was observed in the activities ascribed to the NDH-1MS complex, i.e., CO2 uptake and cyclic electron transport. This may suggest that the NDH-1MS complex has the third, currently unknown function under photomixotrophic conditions.
  SPRINGER, English, Scientific journal
  DOI：https://doi.org/10.1007/s11120-015-0143-8
  DOI ID：10.1007/s11120-015-0143-8, ISSN：0166-8595, eISSN：1573-5079, PubMed ID：25869635, Web of Science ID：WOS:000362006900025
• Oxidation of translation factor EF-G transiently retards the translational elongation cycle in Escherichia coli　　　　　　　　　　　　　　　
  Takanori Nagano; Rayakorn Yutthanasirikul; Yukako Hihara; Toru Hisabori; Takashi Kanamori; Nono Takeuchi; Takuya Ueda; Yoshitaka Nishiyama
  JOURNAL OF BIOCHEMISTRY, Volume：158, Number：2, First page：165, Last page：172, Aug. 2015, [Reviewed]
  In Escherichia coli, elongation factor G (EF-G), a key protein in translational elongation, is particularly susceptible to oxidation. We demonstrated previously that EF-G is inactivated upon formation of an intramolecular disulphide bond. However, the details of the mechanism by which the oxidation of EF-G inhibits the function of EF-G on the ribosome remain to be elucidated. When we oxidized EF-G with hydrogen peroxide, neither the insertion of EF-G into the ribosome nor single-cycle translocation activity in vitro was affected. However, the GTPase activity and the dissociation of EF-G from the ribosome were suppressed when EF-G was oxidized. The synthesis of longer peptides was suppressed to a greater extent than that of a shorter peptide when EF-G was oxidized. Thus, the formation of the disulphide bond in EF-G might interfere with the hydrolysis of GTP that is coupled with dissociation of EF-G from the ribosome and might thereby retard the turnover of EF-G within the translational machinery. When we added thioredoxin to the suppressed translation system that included oxidized EF-G, translational activity was almost immediately restored. We propose that oxidation of EF-G might provide a regulatory mechanism for transient and reversible suppression of translation in E. coli under oxidative stress.
  OXFORD UNIV PRESS, English, Scientific journal
  DOI：https://doi.org/10.1093/jb/mvv026
  DOI ID：10.1093/jb/mvv026, ISSN：0021-924X, eISSN：1756-2651, PubMed ID：25742739, Web of Science ID：WOS:000359684400008
• Zeaxanthin and Echinenone Protect the Repair of Photosystem II from Inhibition by Singlet Oxygen in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Yuri Kusama; Shuhei Inoue; Haruhiko Jimbo; Shinichi Takaichi; Kintake Sonoike; Yukako Hihara; Yoshitaka Nishiyama
  PLANT AND CELL PHYSIOLOGY, Volume：56, Number：5, First page：906, Last page：916, May 2015, [Reviewed]
  Carotenoids are important components of antioxidative systems in photosynthetic organisms. We investigated the roles of zeaxanthin and echinenone in the protection of PSII from photoinhibition in Synechocystis sp. PCC 6803, using mutants of the cyanobacterium that lack these carotenoids. The activity of PSII in mutant cells deficient in either zeaxanthin or echinenone was more sensitive to strong light than the activity in wild-type cells, and the activity in mutant cells deficient in both carotenoids was hypersensitive to strong light, indicating that the absence of these carotenoids increased the extent of photoinhibition. Nonetheless, the rate of photodamage to PSII, as measured in the presence of chloramphenicol, which blocks the repair of PSII, was unaffected by the absence of either carotenoid, suggesting that these carotenoids might act by protecting the repair of PSII. Knockout of the gene for the so-called orange carotenoid protein (OCP), in which the 3'-hydroxyechinenone cofactor, a derivative of echinenone, is responsible for the thermal dissipation of excitation energy, increased the extent of photoinhibition but did not affect photodamage, suggesting that thermal dissipation also protects the repair of PSII. In mutant cells lacking OCP, as well as those lacking zeaxanthin and echinenone, the production of singlet oxygen was stimulated and the synthesis de novo of various proteins, including the D1 protein, was markedly suppressed under strong light. These observations suggest that the carotenoids and thermal dissipation might protect the repair of photodamaged PSII by depressing the levels of singlet oxygen that inhibits protein synthesis.
  OXFORD UNIV PRESS, English, Scientific journal
  DOI：https://doi.org/10.1093/pcp/pcv018
  DOI ID：10.1093/pcp/pcv018, ISSN：0032-0781, eISSN：1471-9053, PubMed ID：25663484, Web of Science ID：WOS:000355313900009
• Identification of OmpR-Family Response Regulators Interacting with Thioredoxin in the Cyanobacterium Synechocystis sp. PCC 6803 (vol 19, e0119107, 2015)　　　　　　　　　　　　　　　
  Taro Kadowaki; Yoshitaka Nishiyama; Toru Hisabori; Yukako Hihara
  PLOS ONE, Volume：10, Number：4, First page：e0119107, Apr. 2015, [Reviewed]
  PUBLIC LIBRARY SCIENCE, English
  DOI：https://doi.org/10.1371/journal.pone.0124571
  DOI ID：10.1371/journal.pone.0124571, ISSN：1932-6203, PubMed ID：25774906, Web of Science ID：WOS:000352845100265
• Correction: identification of OmpR-family response regulators interacting with thioredoxin in the cyanobacterium Synechocystis sp. PCC 6803.　　　　　　　　　　　　　　　
  Kadowaki T; Nishiyama Y; Hisabori T; Hihara Y
  PloS one, Volume：10, Number：4, First page：e0124571, 2015, [Reviewed]
  DOI：https://doi.org/10.1371/journal.pone.0124571
  DOI ID：10.1371/journal.pone.0124571, PubMed ID：25875789
• The effects of dark incubation on cellular metabolism of the wild type cyanobacterium Synechocystis sp. PCC 6803 and a mutant lacking the transcriptional regulator cyAbrB2　　　　　　　　　　　　　　　
  Masamitsu Hanai; Yusuke Sato; Atsuko Miyagi; Maki Kawai-Yamada; Kyoko Tanaka; Yasuko Kaneko; Yoshitaka Nishiyama; Yukako Hihara
  Life, Volume：4, Number：4, First page：770, Last page：787, Nov. 2014, [Reviewed]
  The cyAbrB2 transcriptional regulator is essential for active sugar catabolism in Synechocystis sp. PCC 6 803 grown under light conditions. In the light-growncyabrB2-disrupted mutant, glycogen granules and sugar phosphates corresponding to early steps in the glycolytic pathway accumulated to higher levels than those in the wild-type (WT) strain, whereas the amounts of 3-phosphoglycerate, phosphoenolpyruvate and ribulose 1,5-bisphosphate were significantly lower. We further determined that accumulated glycogen granules in the mutant could be actively catabolized under dark conditions. Differences in metabolite levels between WT and the mutant became less substantial during dark incubation due to a general quantitative decrease in metabolite levels. Notable exceptions, however, were increases in 2-oxoglutarate, histidine, ornithine and citrulline in the WT but not in the mutant. The amounts of cyAbrBs were highly responsive to the availability of light both in transcript and protein levels. When grown under light-dark cycle conditions, diurnal oscillatory pattern of glycogen content of the mutant was lost after the second dark period. These observations indicate that cyAbrB2 is dispensable for activation of sugar catabolism under dark conditions but involved in the proper switching between day and night metabolisms.
  MDPI AG, English, Scientific journal
  DOI：https://doi.org/10.3390/life4040770
  DOI ID：10.3390/life4040770, ISSN：2075-1729, PubMed ID：25423139, SCOPUS ID：84938900212
• Revised scheme for the mechanism of photoinhibition and its application to enhance the abiotic stress tolerance of the photosynthetic machinery　　　　　　　　　　　　　　　
  Yoshitaka Nishiyama; Norio Murata
  APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, Volume：98, Number：21, First page：8777, Last page：8796, Nov. 2014, [Reviewed]
  When photosynthetic organisms are exposed to abiotic stress, their photosynthetic activity is significantly depressed. In particular, photosystem II (PSII) in the photosynthetic machinery is readily inactivated under strong light and this phenomenon is referred to as photoinhibition of PSII. Other types of abiotic stress act synergistically with light stress to accelerate photoinhibition. Recent studies of photoinhibition have revealed that light stress damages PSII directly, whereas other abiotic stresses act exclusively to inhibit the repair of PSII after light-induced damage (photodamage). Such inhibition of repair is associated with suppression, by reactive oxygen species (ROS), of the synthesis of proteins de novo and, in particular, of the D1 protein, and also with the reduced efficiency of repair under stress conditions. Gene-technological improvements in the tolerance of photosynthetic organisms to various abiotic stresses have been achieved via protection of the repair system from ROS and, also, by enhancing the efficiency of repair via facilitation of the turnover of the D1 protein in PSII. In this review, we summarize the current status of research on photoinhibition as it relates to the effects of abiotic stress and we discuss successful strategies that enhance the activity of the repair machinery. In addition, we propose several potential methods for activating the repair system by gene-technological methods.
  SPRINGER, English
  DOI：https://doi.org/10.1007/s00253-014-6020-0
  DOI ID：10.1007/s00253-014-6020-0, ISSN：0175-7598, eISSN：1432-0614, PubMed ID：25139449, Web of Science ID：WOS:000343904700001
• Expression of a highly active catalase VktA in the cyanobacterium Synechococcus elongatus PCC 7942 alleviates the photoinhibition of photosystem II　　　　　　　　　　　　　　　
  Haruhiko Jimbo; Akiko Noda; Hidenori Hayashi; Takanori Nagano; Isao Yumoto; Yoshitake Orikasa; Hidetoshi Okuyama; Yoshitaka Nishiyama
  PHOTOSYNTHESIS RESEARCH, Volume：117, Number：1-3, First page：509, Last page：515, Nov. 2013, [Reviewed]
  The repair of photosystem II (PSII) after photodamage is particularly sensitive to reactive oxygen species-such as H2O2, which is abundantly produced during the photoinhibition of PSII. In the present study, we generated a transformant of the cyanobacterium Synechococcus elongatus PCC 7942 that expressed a highly active catalase, VktA, which is derived from a facultatively psychrophilic bacterium Vibrio rumoiensis, and examined the effect of expression of VktA on the photoinhibition of PSII. The activity of PSII in transformed cells declined much more slowly than in wild-type cells when cells were exposed to strong light in the presence of H2O2. However, the rate of photodamage to PSII, as monitored in the presence of chloramphenicol, was the same in the two lines of cells, suggesting that the repair of PSII was protected by the expression of VktA. The de novo synthesis of the D1 protein, which is required for the repair of PSII, was activated in transformed cells under the same stress conditions. Similar protection of the repair of PSII in transformed cells was also observed under strong light at a relatively low temperature. Thus, the expression of the highly active catalase mitigates photoinhibition of PSII by protecting protein synthesis against damage by H2O2 with subsequent enhancement of the repair of PSII.
  SPRINGER, English, Scientific journal
  DOI：https://doi.org/10.1007/s11120-013-9804-7
  DOI ID：10.1007/s11120-013-9804-7, ISSN：0166-8595, eISSN：1573-5079, PubMed ID：23456267, Web of Science ID：WOS:000326604900037
• Characterization of the Plastidic Phosphate Translocators in the Inducible Crassulacean Acid Metabolism Plant Mesembryanthemum crystallinum　　　　　　　　　　　　　　　
  Shin Kore-eda; Akira Nozawa; Yusuke Okada; Kazuki Takashi; Muhammad Abul Kalam Azad; Jun-ichi Ohnishi; Yoshitaka Nishiyama; Yuzuru Tozawa
  BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, Volume：77, Number：7, First page：1511, Last page：1516, Jul. 2013, [Reviewed]
  In plant Mesembryanthemum crystallinum, which has the inducible crassulacean acid metabolism (CAM), isoforms of plastidic phosphate translocators (pPTs) are categorized into three subfamilies: the triose phosphate/phosphate translocator (McTPT1), the phosphoenolpyruvate/phosphate translocator (McPPT1), and the glucose 6-phosphate/phosphate translocator (McGPT1 and McGPT2). In order to elucidate the physiological roles of these pPTs in M. crystallinum, we determined the substrate specificity of each pPT isoform. The substrate specificities of McTPT1, McPPT1, and McGPT1 showed overall similarities to those of orthologs that have been characterized. In contrast, for glucose 6-phosphate, McGPT2 showed higher selectivity than McGPT1 and other GPT orthologs. Because the expression of McGTP2 is specific to CAM while that of McGTP1 is constitutively expressed in both the C-3- and the CAM-state in M. crystallinum, we propose that McGPT2 functions as a CAM system-specific GPT in this plant.
  TAYLOR & FRANCIS LTD, English, Scientific journal
  DOI：https://doi.org/10.1271/bbb.130174
  DOI ID：10.1271/bbb.130174, ISSN：0916-8451, eISSN：1347-6947, PubMed ID：23832369, Web of Science ID：WOS:000323533800026
• Deletion of the Transcriptional Regulator cyAbrB2 Deregulates Primary Carbon Metabolism in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Yuki Kaniya; Ayumi Kizawa; Atsuko Miyagi; Maki Kawai-Yamada; Hirofumi Uchimiya; Yasuko Kaneko; Yoshikata Nishiyama; Yukako Hihara
  PLANT PHYSIOLOGY, Volume：162, Number：2, First page：1153, Last page：1163, Jun. 2013, [Reviewed]
  cyAbrB is a transcriptional regulator unique to and highly conserved among cyanobacterial species. A gene-disrupted mutant of cyabrB2 (sll0822) in Synechocystis sp. PCC 6803 exhibited severe growth inhibition and abnormal accumulation of glycogen granules within cells under photomixotrophic conditions. Within 6 h after the shift to photomixotrophic conditions, sodium bicarbonate-dependent oxygen evolution activity markedly declined in the Delta cyabrB2 mutant, but the decrease in methyl viologen-dependent electron transport activity was much smaller, indicating inhibition in carbon dioxide fixation. Decreases in the transcript levels of several genes related to sugar catabolism, carbon dioxide fixation, and nitrogen metabolism were also observed within 6 h. Metabolome analysis by capillary electrophoresis mass spectrometry revealed that several metabolites accumulated differently in the wild-type and mutant strains. For example, the amounts of pyruvate and 2-oxoglutarate (2OG) were significantly lower in the mutant than in the wild type, irrespective of trophic conditions. The growth rate of the Delta cyabrB2 mutant was restored to a level comparable to that under photoautotrophic conditions by addition of 2OG to the growth medium under photomixotrophic conditions. Activities of various metabolic processes, including carbon dioxide fixation, respiration, and nitrogen assimilation, seemed to be enhanced by 2OG addition. These observations suggest that cyAbrB2 is essential for the active transcription of genes related to carbon and nitrogen metabolism upon a shift to photomixotrophic conditions. Deletion of cyAbrB2 is likely to deregulate the partition of carbon between storage forms and soluble forms used for biosynthetic purposes. This disorder may cause inactivation of cellular metabolism, excess accumulation of reducing equivalents, and subsequent loss of viability under photomixotrophic conditions.
  AMER SOC PLANT BIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.113.218784
  DOI ID：10.1104/pp.113.218784, ISSN：0032-0889, Web of Science ID：WOS:000319819900047
• The mechanism of photoinhibition in vivo: re-evaluation of the roles of catalase, α-tocopherol, non-photochemical quenching, and electron transport.　　　　　　　　　　　　　　　
  Murata N; Allakhverdiev SI; Nishiyama Y
  Biochimica et Biophysica Acta, Volume：1817, Number：8, First page：1127, Last page：1133, Aug. 2012, [Reviewed]
  DOI：https://doi.org/10.1016/j.bbabio.2012.02.020
  DOI ID：10.1016/j.bbabio.2012.02.020, ISSN：0006-3002, PubMed ID：22387427
• Elongation Factor G Is a Critical Target during Oxidative Damage to the Translation System of Escherichia coli　　　　　　　　　　　　　　　
  Takanori Nagano; Kouji Kojima; Toru Hisabori; Hidenori Hayashi; Eugene Hayato Morita; Takashi Kanamori; Tomoko Miyagi; Takuya Ueda; Yoshitaka Nishiyama
  JOURNAL OF BIOLOGICAL CHEMISTRY, Volume：287, Number：34, First page：28697, Last page：28704, Aug. 2012, [Reviewed]
  Elongation factor G (EF-G), a key protein in translational elongation, is known to be particularly susceptible to oxidation in Escherichia coli. However, neither the mechanism of the oxidation of EF-G nor the influence of its oxidation on translation is fully understood. In the present study, we investigated the effects of oxidants on the chemical properties and function of EF-G using a translation system in vitro derived from E. coli. Treatment of EF-G with 0.5 mM H2O2 resulted in the complete loss of translational activity. The inactivation of EF-G by H2O2 was attributable to the oxidation of two specific cysteine residues, namely, Cys(114) and Cys(266), and subsequent formation of an intramolecular disulfide bond. Replacement of Cys(114) by serine rendered EF-G insensitive to oxidation and inactivation by H2O2. Furthermore, generation of the translation system in vitro with the mutated EF-G protected the entire translation system from oxidation, suggesting that EF-G might be a primary target of oxidation within the translation system. Oxidized EF-G was reactivated via reduction of the disulfide bond by thioredoxin, a ubiquitous protein that mediates dithiol-disulfide exchange. Our observations indicate that the translational machinery in E. coli is regulated, in part, by the redox state of EF-G, which might depend on the balance between the supply of reducing power and the degree of oxidative stress.
  AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, English, Scientific journal
  DOI：https://doi.org/10.1074/jbc.M112.378067
  DOI ID：10.1074/jbc.M112.378067, ISSN：0021-9258, PubMed ID：22773838, Web of Science ID：WOS:000308074600043
• A change in the sensitivity of elongation factor G to oxidation protects photosystem II from photoinhibition in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Kayoko Ejima; Tomoko Kawaharada; Shuhei Inoue; Kouji Kojima; Yoshitaka Nishiyama
  FEBS LETTERS, Volume：586, Number：6, First page：778, Last page：783, Mar. 2012, [Reviewed]
  The repair of photosystem II (PSII) after photodamage is particularly sensitive to oxidative stress and inhibition of such repair is associated with the oxidation of specific cysteine residues in elongation factor G (EF-G), a key translation factor, in the cyanobacterium Synechocystis sp. PCC 6803. Expression of mutated EF-G with a target cysteine residue replaced by serine in Synechocystis resulted in the protection of PSII from photoinhibition. This protection was attributable to the enhanced repair of PSII via acceleration of the synthesis of the D1 protein, which might have been due to reduced sensitivity of protein synthesis to oxidative stress. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.febslet.2012.01.042
  DOI ID：10.1016/j.febslet.2012.01.042, ISSN：0014-5793, PubMed ID：22300643, Web of Science ID：WOS:000301924600021
• Comparative study of the different mechanisms for zinc ion stress sensing in two cyanobacterial strains, Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  Eugene Hayato Morita; Satsuki Kawamoto; Shunnosuke Abe; Yoshitaka Nishiyama; Takahisa Ikegami; Hidenori Hayashi
  Biophysics (Japan), Volume：8, First page：103, Last page：109, 2012, [Reviewed]
  In response to an increased level of Zn2+, Synechococcus sp. PCC 7942 expresses SmtA, a metallothionein-like metal-chelating protein, while Synechocystis sp. PCC 6803 expresses ZiaA, a transporter of Zn2+. The gene expression of these proteins is regulated by repressor protein, SmtB and ZiaR, respectively. In spite of contributing to different response systems, both repressor proteins belong to the ArsR family and are highly homologous to each other. To understand the different systems responsible for dealing with excess Zn2+, we examined the cis-elements in the promoter regions of smtA and ziaA, as well as the binding affinities of recombinant SmtB and ZiaR proteins. The operator/promoter region of smtA included two palindromic sequences and that of ziaA included one. Electrophoretic mobility shift assay revealed that SmtB formed four different complexes with the operator/promoter region of smtA, whereas it formed only two different complexes with the corresponding region of ziaA. For ZiaR, the corresponding results were quite the same as those for SmtB. Furthermore, the complex formation between SmtB and operator/promoter regions is inhibited in the presence of Zn2+ at higher concentrations than 16 μM. On the other hand, the corresponding Zn2+ concentration is 128 μM. These results demonstrate that the degrees of protein- DNA complex formation between repressor proteins and the operator/promoter regions of regulated genes depend on the structures of the operator/promoter regions, and the effects of Zn2+ on the dissociation of these complexes are mainly associated with the structures of the repressors. © 2012 TTHE BIOPHYSICAL SOCIETY OF JAPAN.
  English, Scientific journal
  DOI：https://doi.org/10.2142/biophysics.8.103
  DOI ID：10.2142/biophysics.8.103, ISSN：1349-2942, PubMed ID：27493526, SCOPUS ID：84864207857
• Protein synthesis is the primary target of reactive oxygen species in the photoinhibition of photosystem II　　　　　　　　　　　　　　　
  Yoshitaka Nishiyama; Suleyman I. Allakhverdiev; Norio Murata
  PHYSIOLOGIA PLANTARUM, Volume：142, Number：1, First page：35, Last page：46, May 2011, [Reviewed]
  Photoinhibition of photosystem II (PSII) occurs when the rate of photodamage to PSII exceeds the rate of the repair of photodamaged PSII. Recent examination of photoinhibition by separate determinations of photodamage and repair has revealed that the rate of photodamage to PSII is directly proportional to the intensity of incident light and that the repair of PSII is particularly sensitive to the inactivation by reactive oxygen species (ROS). The ROS-induced inactivation of repair is attributable to the suppression of the synthesis de novo of proteins, such as the D1 protein, that are required for the repair of PSII at the level of translational elongation. Furthermore, molecular analysis has revealed that the ROS-induced suppression of protein synthesis is associated with the specific inactivation of elongation factor G via the formation of an intramolecular disulfide bond. Impairment of various mechanisms that protect PSII against photoinhibition, including photorespiration, thermal dissipation of excitation energy, and the cyclic transport of electrons, decreases the rate of repair of PSII via the suppression of protein synthesis. In this review, we present a newly established model of the mechanism and the physiological significance of repair in the regulation of the photoinhibition of PSII.
  WILEY-BLACKWELL, English, Scientific journal
  DOI：https://doi.org/10.1111/j.1399-3054.2011.01457.x
  DOI ID：10.1111/j.1399-3054.2011.01457.x, ISSN：0031-9317, PubMed ID：21320129, Web of Science ID：WOS:000289470800005
• Protection by alpha-tocopherol of the repair of photosystem II during photoinhibition in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Shuhei Inoue; Kayoko Ejima; Eri Iwai; Hidenori Hayashi; Jens Appel; Esa Tyystjarvi; Norio Murata; Yoshitaka Nishiyama
  BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Volume：1807, Number：2, First page：236, Last page：241, Feb. 2011, [Reviewed]
  alpha-Tocopherol is a lipophilic antioxidant that is an efficient scavenger of singlet oxygen. We investigated the role of alpha-tocopherol in the protection of photosystem II (PSII) from photoinhibition using a mutant of the cyanobacterium Synechocystis sp. PCC 6803 that is deficient in the biosynthesis of a-tocopherol. The activity of PSII in mutant cells was more sensitive to inactivation by strong light than that in wild-type cells, indicating that lack of alpha-tocopherol enhances the extent of photoinhibition. However, the rate of photodamage to PSII, as measured in the presence of chloramphenicol, which blocks the repair of PSII, did not differ between the two lines of cells. By contrast, the repair of PSII from photodamage was suppressed in mutant cells. Addition of alpha-tocopherol to cultures of mutant cells returned the extent of photoinhibition to that in wild-type cells, without any effect on photodamage. The synthesis de novo of various proteins, including the D1 protein that plays a central role in the repair of PSII, was suppressed in mutant cells under strong light. These observations suggest that alpha-tocopherol promotes the repair of photodamaged PSII by protecting the synthesis de novo of the proteins that are required for recovery from inhibition by singlet oxygen. (C) 2010 Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.bbabio.2010.11.003
  DOI ID：10.1016/j.bbabio.2010.11.003, ISSN：0005-2728, Web of Science ID：WOS:000286681400007
• Protection by α-tocopherol of the repair of photosystem II during photoinhibition in Synechocystis sp. PCC 6803.　　　　　　　　　　　　　　　
  Inoue S; Ejima K; Iwai E; Hayashi H; Appel J; Tyystjärvi E; Murata N; Nishiyama Y
  Biochimica et Biophysica Acta, Volume：1807, Number：2, First page：236, Last page：241, Feb. 2011, [Reviewed]
  DOI：https://doi.org/10.1016/j.bbabio.2010.11.003
  DOI ID：10.1016/j.bbabio.2010.11.003, ISSN：0006-3002, PubMed ID：21074511
• The PedR transcriptional regulator interacts with thioredoxin to connect photosynthesis with gene expression in cyanobacteria　　　　　　　　　　　　　　　
  Mayumi Horiuchi; Kinu Nakamura; Kouji Kojima; Yoshitaka Nishiyama; Wakako Hatakeyama; Toru Hisabori; Yukako Hihara
  BIOCHEMICAL JOURNAL, Volume：431, Number：1, First page：135, Last page：140, Oct. 2010, [Reviewed]
  The redox state of the photosynthetic electron transport chain acts as a critical sensing mechanism by regulating the transcription of key genes involved in the acclimation response to a change in the environment. In the present study we show that the small LuxR-type regulator PedR interacts with Trx (thioredoxin) to achieve photosynthetic electron-transport-dependent transcriptional regulation in the cyanobacterium Synechocystis sp. PCC 6803. TrxM, an isoform of Trx, was isolated as an interacting factor of PedR by pull-down assays. In vitro analysis revealed that the intermolecular disulfide bond formed between Cys(80) residues of the PedR homodimer was reduced by both TrxM and TrxX. It has been shown previously that, although PedR is active under low-light conditions, it becomes transiently inactivated following a shift to high-light conditions, with a concomitant conformational change [Nakamura and Hihara (2006) J. Biol. Chem. 281, 36758-36766]. In the present study, we found that the conformational change of PedR and the change in the transcript level of its target gene were minimal when mutants of Synechocystis that lack ferredoxin-Trx reductase or NADPH-Trx reductase were exposed to high levels of light. These results indicate that the reduction of PedR by Trx causes transient inactivation of PedR upon the shift of cyanobacterial cells to high-light conditions.
  PORTLAND PRESS LTD, English, Scientific journal
  DOI：https://doi.org/10.1042/BJ20100789
  DOI ID：10.1042/BJ20100789, ISSN：0264-6021, PubMed ID：20662766, Web of Science ID：WOS:000282852800014
• Synthesis of fatty acids de novo is required for photosynthetic acclimation of Synechocystis sp PCC 6803 to high temperature　　　　　　　　　　　　　　　
  Yohei Nanjo; Naoki Mizusawa; Hajime Wada; Antoni R. Slabas; Hidenori Hayashi; Yoshitaka Nishiyama
  BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Volume：1797, Number：8, First page：1483, Last page：1490, Aug. 2010, [Reviewed]
  The role of fatty acid synthesis in the acclimation of the photosynthetic machinery to high temperature was investigated in a mutant of the cyanobacterium Synechocystis sp. PCC 6803 that had a lower than wild-type level of enoyl-(acyl-carrier-protein) reductase Fabl, a key component of the type-II fatty acid synthase system. The mutant exhibited marked impairment in the tolerance and acclimation of cells to high temperature: photoautotrophic growth of the mutant was severely inhibited at 40 degrees C. Moreover, mutant cells were unable to achieve wild-type enhancement of the thermal stability of photosystem II (PSII) when the growth temperature was raised from 25 degrees C to 38 degrees C. Enhancement of the thermal stability of PSII was abolished when wild-type cells were treated with triclosan, a specific inhibitor of Fabl, and the enhancement of thermal stability was also blocked in darkness and in the presence of chloramphenicol. Analysis of fatty acids in thylakoid membranes revealed that levels of unsaturated fatty acids did not differ between mutant and wild-type cells, indicating that the saturation of fatty acids in membrane lipids might not be responsible for the enhancement of thermal stability at elevated temperatures. Our observations suggest that the synthesis de novo of fatty acids, as well as proteins, is required for the enhancement of the thermal stability of PSII during the acclimation of Synechocystis cells to high temperature. (C) 2010 Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.bbabio.2010.03.014
  DOI ID：10.1016/j.bbabio.2010.03.014, ISSN：0005-2728, Web of Science ID：WOS:000279888700016
• Synthesis of fatty acids de novo is required for photosynthetic acclimation of Synechocystis sp. PCC 6803 to high temperature.　　　　　　　　　　　　　　　
  Nanjo Y; Mizusawa N; Wada H; Slabas AR; Hayashi H; Nishiyama Y
  Biochimica et Biophysica Acta, Volume：1797, Number：8, First page：1483, Last page：1490, Aug. 2010, [Reviewed]
  DOI：https://doi.org/10.1016/j.bbabio.2010.03.014
  DOI ID：10.1016/j.bbabio.2010.03.014, ISSN：0006-3002, PubMed ID：20303926
• Differential proteomic analysis using iTRAQ reveals changes in thylakoids associated with Photosystem II-acquired thermotolerance in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  John G. Rowland; William J. Simon; Yoshitaka Nishiyama; Antoni R. Slabas
  PROTEOMICS, Volume：10, Number：10, First page：1917, Last page：1929, May 2010, [Reviewed]
  Growth temperature has a marked influence on the thermotolerance of photosystem II (PSII), which is the most heat-sensitive component of photosynthesis. Using Synechocystis sp. PCC 6803 we have established that thylakoids isolated from cells grown at 38 degrees C have a greater degree of thermotolerance than those isolated from cells grown at 25 degrees C. Reconstitution experiments using Triton X-100 protein extracts of these thylakoids added to Triton-treated thylakoid membranes further indicated that the 38 degrees C Triton extract contains proteins that are directly capable of enhancing PSII thermotolerance. We have used 4-plex iTRAQ, extensive off-line fractionation and sample re-injection to comprehensively identify the differences between these two preparations that may be responsible for the observed effects on PSII thermotolerance. This has resulted in the reproducible identification of 168 proteins out of a total of 385 distinct proteins. Our results have identified 15 proteins whose levels are increased in extracts that result in increased thermotolerance of PSII and 33 proteins whose levels decrease. Notably, components of the cytochrome b(6)/f and NADH dehydrogenase complexes, crucial components in electron transport, are approximately twofold more abundant in 38 degrees C thylakoid extracts. The possible biological importance of these changes is discussed.
  WILEY-BLACKWELL, English, Scientific journal
  DOI：https://doi.org/10.1002/pmic.200900337
  DOI ID：10.1002/pmic.200900337, ISSN：1615-9853, eISSN：1615-9861, PubMed ID：20336677, Web of Science ID：WOS:000278494100002
• Regulation of Translation by the Redox State of Elongation Factor G in the Cyanobacterium Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Kouji Kojima; Ken Motohashi; Takuya Morota; Masaru Oshita; Toru Hisabori; Hidenori Hayashi; Yoshitaka Nishiyama
  JOURNAL OF BIOLOGICAL CHEMISTRY, Volume：284, Number：28, First page：18685, Last page：18691, Jul. 2009, [Reviewed]
  Elongation factor G (EF-G), a key protein in translational elongation, was identified as a primary target of inactivation by reactive oxygen species within the translational machinery of the cyanobacterium Synechocystis sp. PCC 6803 (Kojima, K., Oshita, M., Nanjo, Y., Kasai, K., Tozawa, Y., Hayashi, H., and Nishiyama, Y. (2007) Mol. Microbiol. 65, 936-947). In the present study, we found that inactivation of EF-G (Slr1463) by H(2)O(2) was attributable to the oxidation of two specific cysteine residues and formation of a disulfide bond. Substitution of these cysteine residues by serine residues protected EF-G from inactivation by H(2)O(2) and allowed the EF-G to mediate translation in a translation system in vitro that had been prepared from Synechocystis. The disulfide bond in oxidized EF-G was reduced by thioredoxin, and the resultant reduced form of EF-G regained the activity to mediate translation in vitro. Western blotting analysis showed that levels of the oxidized form of EF-G increased under strong light in a mutant that lacked NADPH-thioredoxin reductase, indicating that EF-G is reduced by thioredoxin in vivo. These observations suggest that the translational machinery is regulated by the redox state of EF-G, which is oxidized by reactive oxygen species and reduced by thioredoxin, a transmitter of reducing signals generated by the photosynthetic transport of electrons.
  AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, English, Scientific journal
  DOI：https://doi.org/10.1074/jbc.M109.015131
  DOI ID：10.1074/jbc.M109.015131, ISSN：0021-9258, CiNii Articles ID：120002384305, PubMed ID：19447882, Web of Science ID：WOS:000267711500017
• Physiological Impact of Thioredoxin- and Glutaredoxin-Mediated Redox Regulation in Cyanobacteria　　　　　　　　　　　　　　　
  Yoshitaka Nishiyama; Toru Hisabori
  ADVANCES IN BOTANICAL RESEARCH: OXIDATIVE STRESS AND REDOX REGULATION IN PLANTS, VOL 52, Volume：52, First page：187, Last page：+, 2009, [Reviewed]
  Cyanobacteria are photosynthetic bacteria, which are thought to be derived from ancestral oxygen-evolving photosynthetic organisms. Recent progress in proteomics using redox-protein affinity chromatography, two-dimensional electrophoresis and mass spectrometry has improved our understanding of the complicated redox-regulation networks that exist in photosynthetic organisms, and studies with cyanobacteria have made a great contribution to this area. Moreover, a number of remarkable differences relating to redox-regulated proteins between higher plants and cyanobacteria have also been uncovered as a result of these studies. In addition, novel redox-regulation systems that govern gene expression and protein synthesis have also been recently described for cyanobacteria. The redox-regulation system is an important multiphasic control system that ensures cell viability for this photosynthetic organism.
  ACADEMIC PRESS LTD-ELSEVIER SCIENCE LTD, English, In book
  DOI：https://doi.org/10.1016/S0065-2296(10)52007-X
  DOI ID：10.1016/S0065-2296(10)52007-X, ISSN：0065-2296, Web of Science ID：WOS:000271660600007
• Role of elongation factor G in the inhibition of the synthesis of the D1 protein of photosystem II under oxidative stress　　　　　　　　　　　　　　　
  Kojima K; Oshita M; Hayashi H; Nishiyama Y
  Photosynthesis. Energy from the Sun, First page：1319, Last page：1322, 2008, [Reviewed]
  DOI：https://doi.org/10.1007/978-1-4020-6709-9_283
  DOI ID：10.1007/978-1-4020-6709-9_283
• Glycinebetaine alleviates the inhibitory repair of photosystem II effect of moderate heat stress on the during photoinhibition　　　　　　　　　　　　　　　
  Suleyman I. Allakhverdiev; Dmitry A. Los; Prasanna Mohanty; Yoshitaka Nishiyama; Norio Murata
  BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Volume：1767, Number：12, First page：1363, Last page：1371, Dec. 2007, [Reviewed]
  Transformation with the bacterial gene codA for choline oxidase allows Synechococcus sp. PCC 7942 cells to accumulate glycinebetaine when choline is supplemented exogenously. First, we observed two types of protective effect of glycinebetaine against beat-induced inactivation of photosystem II (PSII) in darkness; the codA transgene shifted the temperature range of inactivation of the oxygen-evolving complex from 40-52 degrees C (with half inactivation at 46 degrees C) to 46-60 degrees C (with half inactivation at 54 degrees C) and that of the photochemical reaction center from 44-55 degrees C (with half inactivation at 51 degrees C) to 52-63 degrees C (with half inactivation at 58 degrees C). However, in light, PSII was more sensitive to heat stress; when moderate heat stress, such as 40 degrees C, was combined with light stress, PSII was rapidly inactivated, although these stresses, when applied separately, did not inactivate either the oxygen-evolving complex or the photochemical reaction center. Further our studies demonstrated that the moderate heat stress inhibited the repair of PSII during photoinhibition at the site of synthesis de novo of the D1 protein but did not accelerate the photodamage directly. The codA transgene and, thus, the accumulation of glycinebetaine alleviated such an inhibitory effect of moderate heat stress on the repair of PSII by accelerating the synthesis of the D1 protein. We propose a hypothetical scheme for the cyanobacterial photosynthesis that moderate heat stress inhibits the translation machinery and glycinebetaine protects it against the heat-induced inactivation. (C) 2007 Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.bbabio.2007.10.005
  DOI ID：10.1016/j.bbabio.2007.10.005, ISSN：0005-2728, CiNii Articles ID：80018084641, Web of Science ID：WOS:000251916400002
• The plastid sigma factor SIG1 maintains photosystem I activity via regulated expression of the psaA operon in rice chloroplasts　　　　　　　　　　　　　　　
  Yuzuru Tozawa; Masayoshi Teraishi; Tadamasa Sasaki; Kintake Sonoike; Yoshitaka Nishiyama; Mitsuhiro Itaya; Akio Miyao; Hirohiko Hirochika
  PLANT JOURNAL, Volume：52, Number：1, First page：124, Last page：132, Oct. 2007, [Reviewed]
  Sigma factors encoded by the nucleus of plants confer promoter specificity on the bacterial-type RNA polymerase in chloroplasts. We previously showed that transcripts of OsSIG1, which encodes one such sigma factor in rice, accumulate relatively late during leaf development. We have now isolated and characterized two allelic mutants of OsSIG1, in which OsSIG1 is disrupted by insertion of the retrotransposon Tos17, in order to characterize the functions of OsSIG1. The OsSIG1(-/-) plants were found to be fertile but they manifested an approximately one-third reduction in the chlorophyll content of mature leaves. Quantitative RT-PCR and northern blot analyses of chloroplast gene expression revealed that the abundance of transcripts derived from the psaA operon was markedly reduced in OsSIG1(-/-) plants compared with that in wild-type homozygotes. This effect was accompanied by a reduction in the abundance of the core protein complex (PsaA-PsaB) of photosystem I. Analysis of chlorophyll fluorescence also revealed a substantial reduction in the rate of electron transfer from photosystem II to photosystem I in the OsSIG1 mutants. Our results thus indicate that OsSIG1 plays an important role in the maintenance of photosynthetic activity in mature chloroplasts of rice by regulating expression of chloroplast genes for components of photosystem I.
  BLACKWELL PUBLISHING, English, Scientific journal
  DOI：https://doi.org/10.1111/j.1365-313X.2007.03216.x
  DOI ID：10.1111/j.1365-313X.2007.03216.x, ISSN：0960-7412, Web of Science ID：WOS:000249828700011
• Oxidation of elongation factor G inhibits the synthesis of the D1 protein of photosystem II　　　　　　　　　　　　　　　
  Kouji Kojima; Masaru Oshita; Yohei Nanjo; Koji Kasai; Yuzuru Tozawa; Hidenori Hayashi; Yoshitaka Nishiyama
  MOLECULAR MICROBIOLOGY, Volume：65, Number：4, First page：936, Last page：947, Aug. 2007, [Reviewed]
  Oxidative stress inhibits the repair of photodamaged photosystem II (PSII). This inhibition is due initially to the suppression, by reactive oxygen species (ROS), of the synthesis de novo of proteins that are required for the repair of PSII, such as the D1 protein, at the level of translational elongation. To investigate in vitro the mechanisms whereby ROS inhibit translational elongation, we developed a translation system in vitro from the cyanobacterium Synechocystis sp. PCC 6803. The synthesis of the D1 protein in vitro was inhibited by exogenous H2O2. However, the addition of reduced forms of elongation factor G (EF-G), which is known to be particularly sensitive to oxidation, was able to reverse the inhibition of translation. By contrast, the oxidized forms of EF-G failed to restore translational activity. Furthermore, the overexpression of EF-G of Synechocystis in another cyanobacterium Synechococcus sp. PCC 7942 increased the tolerance of cells to H2O2 in terms of protein synthesis. These observations suggest that EF-G might be the primary target, within the translational machinery, of inhibition by ROS.
  WILEY-BLACKWELL, English, Scientific journal
  DOI：https://doi.org/10.1111/j.1365-2958.2007.05836.x
  DOI ID：10.1111/j.1365-2958.2007.05836.x, ISSN：0950-382X, eISSN：1365-2958, CiNii Articles ID：80018361516, PubMed ID：17617168, Web of Science ID：WOS:000249126500007
• Photoinhibition of photosystem II under environmental stress　　　　　　　　　　　　　　　
  Norio Murata; Shunichi Takahashi; Yoshitaka Nishiyama; Suleyman I. Allakhverdiev
  BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Volume：1767, Number：6, First page：414, Last page：421, Jun. 2007, [Reviewed]
  Inhibition of the activity of photosystem II (PSII) under strong light is referred to as photoinhibition. This phenomenon is due to an imbalance between the rate of photodamage to PSII and the rate of the repair of damaged PSII. In the "classical" scheme for the mechanism of photo inhibition, strong light induces the production of reactive oxygen species (ROS), which directly inactivate the photochemical reaction center of PSII. By contrast, in a new scheme, we propose that photodamage is initiated by the direct effect of light on the oxygen-evolving complex and that ROS inhibit the repair of photodamaged PSII by suppressing primarily the synthesis of proteins de novo. The activity of PSII is restricted by a variety of environmental stresses. The effects of environmental stress on damage to and repair of PSII can be examined separately and it appears that environmental stresses, with the exception of strong light, act primarily by inhibiting the repair of PSII. Studies have demonstrated that repair-inhibitory stresses include CO2 limitation, moderate heat, high concentrations of NaCl, and low temperature, each of which suppresses the synthesis of proteins de novo, which is required for the repair of PSII. We postulate that most types of environmental stress inhibit the fixation of CO2 with the resultant generation of ROS, which, in turn, inhibit protein synthesis. (c) 2006 Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.bbabio.2006.11.019
  DOI ID：10.1016/j.bbabio.2006.11.019, ISSN：0005-2728, CiNii Articles ID：80018472094, Web of Science ID：WOS:000247650500003
• Acclimation of photosystem II to high temperature in a suspension culture of soybean (Glycine max) cells requires proteins that are associated with the thylakoid membrane　　　　　　　　　　　　　　　
  Yoshitaka Nishiyama; Kazuya Takechi; Yohei Nanjo; Norio Murata; Hidenori Hayashi
  PHOTOSYNTHESIS RESEARCH, Volume：90, Number：3, First page：223, Last page：232, Dec. 2006, [Reviewed]
  In a study of the responses of photosystem II (PSII) to high temperature in suspension-cultured cells of soybean (Glycine max L. Merr.), we found that high temperatures inactivated PSII via two distinct pathways. Inactivation of PSII by moderately high temperatures, such as 41 degrees C, was reversed upon transfer of cells to 25 degrees C. The recovery of PSII required light, but not the synthesis of proteins de novo. By contrast, temperatures higher than 45 degrees C inactivated PSII irreversibly. An increase in the growth temperature from 25 to 35 degrees C resulted in an upward shift of 3 degrees C in the profile of the heat-induced inactivation of PSII, which indicated that the thermal stability of PSII had been enhanced. This acclimative response was reflected by the properties of isolated thylakoid membranes: PSII in thylakoid membranes from cells that had been grown at 35 degrees C exhibited greater thermal stability than that from cells grown at 25 degrees C. Disruption of the vesicular structure of thylakoid membranes with 0.05% Triton X-100 decreased the thermal stability of PSII to a similar level in both types of thylakoid membrane. Proteins released by Triton X-100 from thylakoid membranes from cells grown at 35 degrees C were able to increase the thermal stability of Triton-treated thylakoid membranes. These observations suggest that proteins that are associated with thylakoid membranes might be involved in the enhancement of the thermal stability of PSII.
  SPRINGER, English, Scientific journal
  DOI：https://doi.org/10.1007/s11120-007-9138-4
  DOI ID：10.1007/s11120-007-9138-4, ISSN：0166-8595, Web of Science ID：WOS:000244725000004
• A new paradigm for the action of reactive oxygen species in the photoinhibition of photosystem II　　　　　　　　　　　　　　　
  Yoshitaka Nishiyama; Suleyman I. Allakhverdiev; Norio Murata
  BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Volume：1757, Number：7, First page：742, Last page：749, Jul. 2006, [Reviewed]
  inhibition of the activity of photosystent II (PSII) under strong light is referred to as photoinhibition. This phenomenon is due to the imbalance between the rate of photodamage to PSII and the rate of the repair of damaged PSII. Photodamage is initiated by the direct effects of light on the oxygen-evolving complex and, thus, photodamage to PSII is unavoidable. Studies of the effects of oxidative stress on photodamage and subsequent repair have revealed that reactive oxygen species (ROS) act primarily by inhibiting the repair of photodamaged PSII and not by damaging PSII directly. Thus, strong light has two distinct effects on PSII; it damages PSII directly and it inhibits the repair of PSII via production of ROS. Investigations of the ROS-induced inhibition of repair have demonstrated that ROS suppress the synthesis de novo of proteins and, in particular, of the D I protein, that are required for the repair of PSII. Moreover, a primary target for inhibition by ROS appears to be the elongation step of translation. Inhibition of the repair of PSII by ROS is accelerated by the deceleration of the Calvin cycle that occurs when the availability of CO2 is limited. In this review, we present a new paradigm for the action of ROS in photoinhibition. (c) 2006 Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English
  DOI：https://doi.org/10.1016/j.bbabio.2006.05.013
  DOI ID：10.1016/j.bbabio.2006.05.013, ISSN：0005-2728, CiNii Articles ID：80019023096, Web of Science ID：WOS:000240053700003
• The rpoH gene encoding heat shock sigma factor sigma(32) of psychrophilic bacterium Colwellia maris　　　　　　　　　　　　　　　
  S Yamauchi; H Okuyama; Y Nishiyama; H Hayashi
  EXTREMOPHILES, Volume：10, Number：2, First page：149, Last page：158, Apr. 2006, [Reviewed]
  The rpoH gene encoding a heat shock sigma factor, sigma(32), was cloned from the psychrophilic bacterium Colwellia maris. The deduced amino acid sequence of sigma(32) from C. maris is more than 60% homologous to that of sigma(32) from mesophilic bacteria. The RpoH box, a 9-amino-acid sequence region (QRKLFFNLR) specific to sigma(32), and two downstream box sequences complementary to a part of 16S rRNA were identified. Primer extension analysis showed that the C. maris rpoH is expressed from only one sigma(70)-type promoter. Northern blot analysis showed that the level of rpoH mRNA was clearly increased at 20 degrees C, a temperature that induces heat shock in this organism. In the presence of an inhibitor of transcriptional initiation, the degradation of rpoH mRNA was much slower at 20 degrees C than at 10 degrees C. Thus, increased stability of the rpoH mRNA might be responsible for the rpoH mRNA accumulation. The predicted secondary structure of the 5'-region of C. maris rpoH mRNA was different from the conserved patterns reported for most mesophilic bacteria, and the base pairing of the downstream boxes appeared to be less stable than that of Escherichia coli rpoH mRNA. Thus, essential features that ensure the HSP expression at a relatively low temperature are embedded in the rpoH gene of psychrophiles.
  SPRINGER TOKYO, English, Scientific journal
  DOI：https://doi.org/10.1007/s00792-005-0485-9
  DOI ID：10.1007/s00792-005-0485-9, ISSN：1431-0651, CiNii Articles ID：120000955292, PubMed ID：16362517, Web of Science ID：WOS:000236973300007
• Very strong UV-A light temporally separates the photoinhibition of photosystem II into light-induced inactivation and repair　　　　　　　　　　　　　　　
  O Zsiros; SI Allakhverdiev; S Higashi; M Watanabe; Y Nishiyama; N Murata
  BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Volume：1757, Number：2, First page：123, Last page：129, Feb. 2006, [Reviewed]
  When organisms that perform oxygenic photosynthesis are exposed to strong visible or UV light, inactivation of photosystem II (PSII) occurs. However, such organisms are able rapidly to repair the photoinactivated PSII. The phenomenon of photoinactivation and repair is known as photoinhibition. Under normal laboratory conditions, the rate of repair is similar to or faster than the rate of photoinactivation, preventing the detailed analysis of photoinactivation and repair as separate processes. We report here that, using strong UV-A light from a laser, we were able to analyze separately the photo inactivation and repair of photosystem II in the cyanobacterium Synechocystis sp. PCC 6803. Very strong UV-A light at 364 nm and a photon flux density of 2600 mu mol photons m(-2) s(-1) inactivated the oxygen-evolving machinery and the photochemical reaction center of PSII within 1 or 2 min before the first step in the repair process, namely, the degradation of the D1 protein, occurred. During subsequent incubation of cells in weak visible light, the activity of PSII recovered fully within 30 min and this process depended on protein synthesis. During subsequent incubation of cells in darkness for 60 min, the D1 protein of the photoinactivated PSII was degraded. Further incubation in weak visible light resulted in the rapid restoration of the activity of PSII. These observations suggest that very strong UV-A light is a useful tool for the analysis of the repair of PSII after photoinactivation. (C) 2006 Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.bbabio.2006.01.004
  DOI ID：10.1016/j.bbabio.2006.01.004, ISSN：0005-2728, CiNii Articles ID：80019293520, Web of Science ID：WOS:000236494200005
• Regulation by environmental conditions of the repair of photosystem II in cyanobacteria　　　　　　　　　　　　　　　
  Nishiyama Y; Allakhverdiev SI; Murata N
  Advances in Photosynthesis and Respiration, First page：193, Last page：203, 2006, [Reviewed]
  DOI：https://doi.org/10.1007/1-4020-3579-9_13
  DOI ID：10.1007/1-4020-3579-9_13
• Systematic characterization of the ADP-ribose pyrophosphatase family in the cyanobacterium Synechocystis sp strain PCC 6803　　　　　　　　　　　　　　　
  K Okuda; H Hayashi; Y Nishiyama
  JOURNAL OF BACTERIOLOGY, Volume：187, Number：14, First page：4984, Last page：4991, Jul. 2005, [Reviewed]
  We have characterized four putative ADP-ribose pyrophosphatases SII1054, SIr0920, SIr1134, and SIr1690 in the cyanobacterium Synechocystis sp. strain PCC 6803. Each of the recombinant proteins was overexpressed in Escherichia coli and purified. SII1054 and Sh-0920 hydrolyzed ADP-ribose specifically, while SIr1134 hydrolyzed not only ADP-ribose but also NADH and flavin adenine dinucleotide. By contrast, Slr1690 showed very low activity for ADP-ribose and had four substitutions of amino acids in the Nudix motif, indicating that Slr1690 is not an active ADP-ribose pyrophosphatase. However, the quadruple mutation of Slr1690, T73G/ I88E/K92E/A94G, which replaced the mutated amino acids with those conserved in the Nudix motif, resulted in a significant (6.1 X 10(2)-fold) increase in the k(cat) value. These results suggest that Slr1690 might have evolved from an active ADP-ribose pyrophosphatase. Functional and clustering analyses suggested that SII1054 is a bacterial type, while the other three and SIr0787, which was characterized previously (Raffaelli et al., FEBS Lett. 444:222-226, 1999), are phylogenetically diverse types that originated from an archaeal Nudix protein via molecular evolutionary mechanisms, such as domain fusion and amino acid substitution.
  AMER SOC MICROBIOLOGY, English, Scientific journal
  DOI：https://doi.org/10.1128/JB.187.14.4984-4991.2005
  DOI ID：10.1128/JB.187.14.4984-4991.2005, ISSN：0021-9193, CiNii Articles ID：80017793187, PubMed ID：15995214, Web of Science ID：WOS:000230350500032
• Two-step mechanism of photodamage to photosystem II: Step 1 occurs at the oxygen-evolving complex and step 2 occurs at the photochemical reaction center　　　　　　　　　　　　　　　
  N Ohnishi; SI Allakhverdiev; S Takahashi; S Higashi; M Watanabe; Y Nishiyama; N Murata
  BIOCHEMISTRY, Volume：44, Number：23, First page：8494, Last page：8499, Jun. 2005, [Reviewed]
  Under strong light, photosystem 11 (PSII) of oxygenic photosynthetic organisms is inactivated, and this phenomenon is called photoinhibition. In a widely accepted model. photoinhibition is induced by excess light energy, which is absorbed by chlorophyll but not utilized in photosynthesis. Using monochromatic light from the Okazaki Large Spectrograph and thylakoid membranes from Thermo-synechococcus elongatus, we observed that UV and blue light inactivated the oxygen-evolving complex much faster than the photochemical reaction center of PSII. These observations suggested that the light-induced damage was associated with a UV- and blue light-absorbing center in the oxygen-evolving complex of PSII. The action spectrum of the primary event in photodamage to PSII revealed the strong effects of UV and blue light and differed considerably from the absorption spectra of chlorophyll and thylakoid membranes. By contrast to the photoinduced inactivation of the oxygen-evolving complex in untreated thylakoid membranes, red light efficiently induced inactivation of the PSII reaction center in Tris-treated thylakoid membranes, and the action spectrum resembled the absorption spectrum of chlorophyll. Our observations suggest that photodamage to PSII occurs in two steps, Step I is the light-induced inactivation of the oxygen-evolving complex. Step 2, occurring after step I is complete, is the inactivation of the PSII reaction center by light absorbed by chlorophyll. We confirmed our model by illumination of untreated thylakoid membranes with blue and UV light, which inactivated the oxygen-evolving complex, and then with red light, which inactivated the photochemical reaction center.
  AMER CHEMICAL SOC, English, Scientific journal
  DOI：https://doi.org/10.1021/bi047518q
  DOI ID：10.1021/bi047518q, ISSN：0006-2960, CiNii Articles ID：80017388797, PubMed ID：15938639, Web of Science ID：WOS:000229725500030
• Inhibition of the repair of Photosystem II by oxidative stress in cyanobacteria　　　　　　　　　　　　　　　
  Y Nishiyama; SI Allakhverdiev; N Murata
  PHOTOSYNTHESIS RESEARCH, Volume：84, Number：1-3, First page：1, Last page：7, Jun. 2005, [Reviewed]
  The activity of Photosystem II (PS II) is severely restricted by a variety of environmental factors and, under environmental stress, is determined by the balance between the rate of damage to PS II and the rate of the repair of damaged PS II. The effects of oxidative stress on damage and repair can be examined separately, and it appears that, while light can damage PS II directly, oxidative stress acts primarily by inhibiting the repair of PS II. Studies in cyanobacteria have demonstrated that oxidative stress suppresses the de novo synthesis of proteins, in particular, the D1 protein, which is required for the repair of PS II.
  SPRINGER, English, Scientific journal
  DOI：https://doi.org/10.1007/s11120-004-6434-0
  DOI ID：10.1007/s11120-004-6434-0, ISSN：0166-8595, Web of Science ID：WOS:000230845200002
• Systematic analysis of the relation of electron transport and ATP synthesis to the photodamage and repair of photosystem II in Synechocystis　　　　　　　　　　　　　　　
  SI Allakhverdiev; Y Nishiyama; S Takahashi; S Miyairi; Suzuki, I; N Murata
  PLANT PHYSIOLOGY, Volume：137, Number：1, First page：263, Last page：273, Jan. 2005, [Reviewed]
  The photosynthetic machinery and, in particular, the photosystem 11 (PSII) complex are susceptible to strong light, and the effects of strong light are referred to as photodamage or photoinhibition. In living organisms, photodamaged PSII is rapidly repaired and, as a result, the extent of photoinhibition represents a balance between rates of photodamage and the repair of PSII. In this study, we examined the roles of electron transport and ATP synthesis in these two processes by monitoring them separately and systematically in the cyanobacterium Synechocystis sp. PCC 6803. We found that the rate of photodamage, which was proportional to light intensity, was unaffected by inhibition of the electron transport in PSII, by acceleration of electron transport in PSI, and by inhibition of ATP synthesis. By contrast, the rate of repair was reduced upon inhibition of the synthesis of ATP either via PSI or PSII. Northern blotting and radiolabeling analysis with [S-35]Met revealed that synthesis of the D1 protein was enhanced by the synthesis of ATP. Our observations suggest that ATP synthesis might regulate the repair of PSII, in particular, at the level of translation of the psbA genes for the precursor to the D1 protein, whereas neither electron transport nor the synthesis of ATP affects the extent of photodamage.
  AMER SOC PLANT BIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.104.054478
  DOI ID：10.1104/pp.104.054478, ISSN：0032-0889, CiNii Articles ID：80017266399, PubMed ID：15618415, Web of Science ID：WOS:000226613100024
• Singlet oxygen inhibits the repair of photosystem II by suppressing the translation elongation of the D1 protein in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Y Nishiyama; SI Allakhverdiev; H Yamamoto; H Hayashi; N Murata
  BIOCHEMISTRY, Volume：43, Number：35, First page：11321, Last page：11330, Sep. 2004, [Reviewed]
  Singlet oxygen, generated during photosynthesis, is a strong oxidant that can, potentially, damage various molecules of biological importance. We investigated the effects in vivo of singlet oxygen on the photodamage to photosystem II (PSII) in the cyanobacterium Synechocystis sp. PCC 6803. Increases in intracellular concentrations of singlet oxygen, caused by the presence of photosensitizers, such as rose bengal and ethyl eosin, stimulated the apparent photodamage to PSII. However, actual photodamage to PSII, as assessed in the presence of chloramphenicol, was unaffected by the production of singlet oxygen. These observations suggest that singlet oxygen produced by added photo sensitizers acts by inhibiting the repair of photodamaged PSII. Labeling of proteins in vivo revealed that singlet oxygen inhibited the synthesis of proteins de novo and, in particular, the synthesis of the D1 protein. Northern blotting analysis indicated that the accumulation of psbA mRNAs, which encode the D1 protein, was unaffected by the production of singlet oxygen. Subcellular localization of polysomes with bound psbA mRNAs suggested that the primary target of singlet oxygen might be the elongation step of translation.
  AMER CHEMICAL SOC, English, Scientific journal
  DOI：https://doi.org/10.1021/bi036178q
  DOI ID：10.1021/bi036178q, ISSN：0006-2960, CiNii Articles ID：80016892300, PubMed ID：15366942, Web of Science ID：WOS:000223708400019
• Gene structure and transcriptional regulation of dnaK and dnaJ genes from a psychrophilic bacterium, Colwellia maris　　　　　　　　　　　　　　　
  S Yamauchi; H Okuyama; Y Nishiyama; H Hayashi
  EXTREMOPHILES, Volume：8, Number：4, First page：283, Last page：290, Aug. 2004, [Reviewed]
  The dnaK and dnaJ genes, encoding heat shock proteins, were cloned from a psychrophilic bacterium, Colwellia maris. Significant homology was evident comparing DnaK and DnaJ of the psychrophilile with the counterparts of mesophilic and thermophilic bacteria. In the DnaJ protein, three conserved regions of the Hsp40 family were observed. A putative promoter similar to the sigma(32) consensus sequence was found upstream of the dnaK gene. The G+C content in the 5'-untranslated region of the dnaK gene was much lower than that in the corresponding region of mesophilic bacteria. Northern-blot analysis and primer-extension analysis showed that both genes were transcribed separately as monocistronic mRNAs. Following several temperature upshifts from 10 to 26degreesC, maximum induction of the dnaK and dnaJ mRNAs was detected at 20degreesC, suggesting that this temperature induces the heat shock response in this bacterium. In addition, the level of the induction of the dnaJ gene was much lower than that of the dnaK gene. These findings together revealed several specific features of the heat shock response at a relatively low temperature in psychrophiles.
  SPRINGER TOKYO, English, Scientific journal
  DOI：https://doi.org/10.1007/s00792-004-0387-2
  DOI ID：10.1007/s00792-004-0387-2, ISSN：1431-0651, Web of Science ID：WOS:000223264300003
• Identification and characterization of NuhA, a novel Nudix hydrolase specific for ADP-ribose in the cyanobacterium Synechococcus sp. PCC 7002　　　　　　　　　　　　　　　
  Kenji Okuda; Yoshitaka Nishiyama; Eugene H. Morita; Hidenori Hayashi
  Biochimica et Biophysica Acta - Proteins and Proteomics, Volume：1699, Number：1-2, First page：245, Last page：252, Jun. 2004, [Reviewed]
  We cloned the gene for a novel Nudix hydrolase in the cyanobacterium Synechococcus sp. PCC 7002 and termed it nuhA. The deduced amino acid sequence of NuhA included the Nudix motif, GX5EX7RELXEEXGV, which is common to Nudix hydrolases, and in addition, a proline at the 15th amino acid from the C-terminus of the Nudix motif, which is characteristic of the subfamily of ADP-ribose pyrophosphatases. The recombinant NuhA with a hexahistidine tag was overexpressed in Escherichia coli and purified. The recombinant NuhA hydrolyzed ADP-ribose specifically among various nucleoside diphosphate derivatives. The hydrolytic activity for ADP-ribose required Mg 2+ and was optimal at pH 9.5. The Vmax and Km values of hydrolysis were 23.6 units mg-1 and 0.094 mM, respectively. NuhA contained an uncharacterized domain in the C-terminal region, termed Pfam-B-3116, which is conserved in several hypothetical proteins. The mutated NuhA deficient in the Pfam-B-3116 domain failed to form the hexamers that are characteristic of NuhA, and exhibited a significantly higher Km value for ADP-ribose, suggesting that the Pfam-B-3116 domain might be responsible for oligomerization of NuhA and full binding affinity for ADP-ribose. These unique features suggest that NuhA is a novel type of ADP-ribose pyrophosphatase. © 2004 Elsevier B.V. All rights reserved.
  Elsevier, English, Scientific journal
  DOI：https://doi.org/10.1016/S1570-9639(04)00069-X
  DOI ID：10.1016/S1570-9639(04)00069-X, ISSN：1570-9639, PubMed ID：15158734, SCOPUS ID：2542459328
• Dissecting a cyanobacterial proteolytic system: efficiency in inducing degradation of the D1 protein of photosystem II in cyanobacteria and plants　　　　　　　　　　　　　　　
  E Kanervo; C Spetea; Y Nishiyama; N Murata; B Andersson; EM Aro
  BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Volume：1607, Number：2-3, First page：131, Last page：140, Dec. 2003, [Reviewed]
  A chromatography fraction, prepared from isolated thylakoids of a fatty acid desaturation mutant (Fad6/desA::Km(I)) of the cyanobacterium Synechocystis 6803, could induce an initial cleavage of the D1 protein in Photosystem II (PSII) particles of Synechocystis 6803 mutant and Synechococcus 7002 wild type as well as in supercomplexes of PSII-light harvesting complex H of spinach. Proteolysis was demonstrated both in darkness and in light as a reduction in the amount of full-length D1 protein or as a production of C-terminal initial degradation fragments. In the Synechocystis mutant, the main degradation fragment was a 10-kDa C-terminal one, indicating an initial cleavage occurring in the cytoplasmic DE-loop of the D1 protein. A protein component of 70-90 kDa. isolated from the chromatographic fraction was found to be involved in the production of this 10-kDa fragment. In spinach, only traces of the corresponding fragment were detected, whereas a 24-kDa C-terminal fragment accumulated, indicating an initial cleavage in the lumenal AB-loop of the D1 protein. Also in Synechocystis the 24-kDa fragment was detected as a faint band. An antibody raised against the Arabidopsis DegP2 protease recognized a 35-kDa band in the proteolytically active chromatographic fraction, suggesting the existence of a lumenal protease that may be the homologue DegP of Synechocystis. The identity of the other protease cleaving the D1 protein in the DE-loop exposed on the stromal (cytoplasmic) side of the membrane is discussed. (C) 2003 Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English, Scientific journal
  DOI：https://doi.org/10.1016/j.bbabio.2003.09.007
  DOI ID：10.1016/j.bbabio.2003.09.007, ISSN：0005-2728, CiNii Articles ID：80016353995, Web of Science ID：WOS:000187241500007
• Refolding from denatured inclusion bodies, purification to homogeneity and simplified assay of MGDG synthases from land plants　　　　　　　　　　　　　　　
  Y Nishiyama; H Hardre-Lienard; S Miras; C Miege; MA Block; F Revah; J Joyard; E Marechal
  PROTEIN EXPRESSION AND PURIFICATION, Volume：31, Number：1, First page：79, Last page：87, Sep. 2003, [Reviewed]
  In plant cells, the synthesis of monogalactosyldiacylglycerol (MGDG) is catalyzed within plastid envelope membranes by MGD proteins. MGDG synthesis was also reported in apicomplexan parasites, a phylum of protists harbouring a plastid that proved essential for the parasite survival. MGD activity is therefore a potent target for herbicidal and anti-parasitic molecules. In this study, we describe a detailed in vitro refolding protocol for denatured recombinant MGD accumulated in inclusion bodies from transformed Escherichia coli. The refolding process was dependent on CHAPS detergent and lipids, such as diacylglycerol and phosphatidylglycerol, as well as bivalent metals. Owing to this refolding procedure, the recombinant MGD protein from spinach was purified to homogeneity, allowing a definite characterization of its non-processivity and an investigation of its dimerization using cross-linking reagents. Additionally, using the portion of recombinant enzyme that accumulates in an active form in bacterial membranes, we developed a miniature assay for high-throughput screening for inhibitors. (C) 2003 Elsevier Science (USA). All rights reserved.
  ACADEMIC PRESS INC ELSEVIER SCIENCE, English, Scientific journal
  DOI：https://doi.org/10.1016/S1046-5928(03)00158-X
  DOI ID：10.1016/S1046-5928(03)00158-X, ISSN：1046-5928, CiNii Articles ID：80016251567, PubMed ID：12963344, Web of Science ID：WOS:000185553900010
• Glycinebetaine protects the D1/D2/Cytb559 complex of photosystem II against photo-induced and heat-induced inactivation　　　　　　　　　　　　　　　
  SI Allakhverdiev; H Hayashi; Y Nishiyama; AG Ivanov; JA Aliev; VV Klimov; N Murata; R Carpentier
  JOURNAL OF PLANT PHYSIOLOGY, Volume：160, Number：1, First page：41, Last page：49, Jan. 2003, [Reviewed]
  The presence of 1.0 mol/L glycinebetaine during isolation of D1/D2/Cytb559 reaction centre (RC) complexes from photosystem 11 (PSII) membrane fragments preserved the photochemical activity, monitored as the light-induced reduction of pheophytin and electron transport from diphenylcarbazide to 2,6-dichlorophenol-indophenol. Glycinebetaine also protected the D1/D2/Cytb559 complexes against strong light-induced damage to the photochemical reactions and the irreversible bleaching of beta-carotene and chlorophyll. The presence of glycinebetaine also enhanced thermotolerance of the D1/D2/Cytb559 complexes isolated in the presence of 1.0 mol/L betaine with an increase in the temperature for 50 % inactivation from 29degreesC to 35degreesC. The results indicate an increased supramolecular structural stability in the presence of glycinebetaine.
  URBAN & FISCHER VERLAG, English, Scientific journal
  DOI：https://doi.org/10.1078/0176-1617-00845
  DOI ID：10.1078/0176-1617-00845, ISSN：0176-1617, Web of Science ID：WOS:000180912800007
• Stabilization of the oxygen-evolving complex of photosystem II by bicarbonate and glycinebetaine in thylakoid and subthylakoid preparations　　　　　　　　　　　　　　　
  VV Klimov; SI Allakhverdiev; Y Nishiyama; AA Khorobrykh; N Murata
  FUNCTIONAL PLANT BIOLOGY, Volume：30, Number：7, First page：797, Last page：803, 2003, [Reviewed]
  The protective effect of 1 M glycinebetaine on thermal inactivation of photosynthetic oxygen evolution in isolated photosystem II membrane fragments from spinach is observed in CO2-free medium in both the presence and absence of added 2 mM bicarbonate. Conversely, the protective effect of 2 mM bicarbonate against thermoinactivation is seen in the absence as well as in the presence of 1 M glycinebetaine. The stabilizing effect of bicarbonate is also observed in thylakoid membranes from Synechococcus sp. PCC 7002 treated with 0.1% Triton X-100, and in unbroken spinach thylakoids. It is shown for the first time that bicarbonate protects the water-oxidizing complex against inactivation induced by pre-incubation of photosystem II membrane fragments (25degreesC) and thylakoids (40degreesC) at low pH (5.0-5.5) in non-bicarbonate-depleted medium. We conclude that the protective effects of glycinebetaine and bicarbonate are of a different nature; glycinebetaine acts as a non-specific, compatible, zwitterionic osmolyte while bicarbonate is considered an essential constituent of the water-oxidizing complex of photosystem II, important for its functioning and stabilization.
  C S I R O PUBLISHING, English, Scientific journal
  DOI：https://doi.org/10.1071/FP03068
  DOI ID：10.1071/FP03068, ISSN：1445-4408, Web of Science ID：WOS:000184615800007
• Studies on the protein-DNA complex formation between the cyanobacterial transcription factors, SmtB and its homologues, functioning as zinc-ion sensors and the recognition DNA sequences　　　　　　　　　　　　　　　
  Morita EH; Wakamatsu M; Kawamoto S; Nishiyama Y; Hayashi H
  Nucleic Acids Res. suppl., Volume：3, First page：203, Last page：204, 2003, [Reviewed]
  PubMed ID：14510451
• Salt stress inhibits the repair of photodamaged photosystem II by suppressing the transcription and translation of psbA genes in Synechocystis　　　　　　　　　　　　　　　
  SI Allakhverdiev; Y Nishiyama; S Miyairi; H Yamamoto; N Inagaki; Y Kanesaki; N Murata
  PLANT PHYSIOLOGY, Volume：130, Number：3, First page：1443, Last page：1453, Nov. 2002, [Reviewed]
  Light stress and salt stress are major environmental factors that limit the efficiency of photosynthesis. However, we have found that the effects of light and salt stress on photosystem II (PSII) in the cyanobacterium Synechocystis sp. PCC 6803 are completely different. Strong light induced photodamage to PSII, whereas salt stress inhibited the repair of the photodamaged PSII and did not accelerate damage to PSII directly. The combination of light and salt stress appeared to inactivate PSII very rapidly as a consequence of their synergistic effects. Radioactive labeling of cells revealed that salt stress inhibited the synthesis of proteins de novo and, in particular, the synthesis of the D1 protein. Northern- and western-blotting analyses demonstrated that salt stress inhibited the transcription and the translation of psbA genes, which encode D1 protein. DNA microarray analysis indicated that the light-induced expression of various genes was suppressed by salt stress. Thus, our results suggest that salt stress inhibits the repair of PSII via suppression of the activities of the transcriptional and translational machinery.
  AMER SOC PLANT BIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.011114
  DOI ID：10.1104/pp.011114, ISSN：0032-0889, CiNii Articles ID：80015655917, PubMed ID：12428009, Web of Science ID：WOS:000179329400036
• Protection of the oxygen-evolving machinery by the extrinsic proteins of photosystem II is essential for development of cellular thermotolerance in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  A Kimura; JJ Eaton-Rye; EH Morita; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：43, Number：8, First page：932, Last page：938, Aug. 2002, [Reviewed]
  The oxygen-evolving machinery of photosystem II in cyanobacteria is associated with three extrinsic proteins: the manganese-stabilizing protein, cytochrome c(550), and PsbU. To elucidate the effect of the presence of these extrinsic proteins on the stabilization of the oxygen-evolving machinery against high-temperature stress, we inactivated the genes for these proteins individually in Synechocystis sp. PCC 6803 by targeted mutagenesis. The thermal stability of the oxygen-evolving machinery decreased in all mutated cells but the extent of the susceptibility to heat inactivation varied between the photosystems lacking the different extrinsic proteins. Cells that lacked either the manganese-stabilizing protein or cytochrome c(550) were unable to enhance the thermal stability of the oxygen-evolving machinery and, moreover, failed to increase cellular thermotolerance when grown at moderately high temperatures. Our findings indicate that the three extrinsic proteins stabilize the oxygen-evolving machinery independently against high-temperature stress and that the thermal stability of the machinery influences cellular thermotolerance.
  OXFORD UNIV PRESS, English, Scientific journal
  DOI：https://doi.org/10.1093/pcp/pcf110
  DOI ID：10.1093/pcp/pcf110, ISSN：0032-0781, CiNii Articles ID：10009500721, PubMed ID：12198196, Web of Science ID：WOS:000177620800012
• No coordinated transcriptional regulation of the sod-kat antioxidative system in Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  Takashi Ushimaru; Yoshitaka Nishiyama; Hidenori Hayashi; Norio Murata
  Journal of Plant Physiology, Volume：159, Number：7, First page：805, Last page：807, 2002, [Reviewed]
  The balanced expression of antioxidative enzymes is believed to be important for effective protection against oxidative stress. The cyanobacterium Synechocystis sp. PCC 6803 possesses the simplest antioxidative system, i.e., a single sod gene (sodB) for SOD and a single kat gene (katG) for catalase/peroxidase, so that it is an ideal model for analyzing the balance of expression. Here we show that sodB expression is induced by various stresses, i.e., O2 -, H2O2, low and high temperatures and high salinity, whereas katG is constitutively expressed. These results suggest that coordinated expression is not essential for antioxidative protection at least in this cyanobacteria. The implications of these phenomena are discussed.
  Elsevier GmbH, English, Scientific journal
  DOI：https://doi.org/10.1078/0176-1617-0812
  DOI ID：10.1078/0176-1617-0812, ISSN：0176-1617, SCOPUS ID：0036074090
• Oxidative stress inhibits the repair of photodamage to the photosynthetic machinery　　　　　　　　　　　　　　　
  Y Nishiyama; H Yamamoto; SI Allakhverdiev; M Inaba; A Yokota; N Murata
  EMBO JOURNAL, Volume：20, Number：20, First page：5587, Last page：5594, Oct. 2001, [Reviewed]
  Absorption of excess light energy by the photosynthetic machinery results in the generation of reactive oxygen species (ROS), such as H2O2. We investigated the effects in vivo of ROS to clarify the nature of the damage caused by such excess light energy to the photosynthetic machinery in the cyanobacterium Synechocystis sp. PCC 6803. Treatments of cyanobacterial cells that supposedly increased intracellular concentrations of ROS apparently stimulated the photodamage to photosystem II by inhibiting the repair of the damage to photosystem II and not by accelerating the photodamage directly. This conclusion was confirmed by the effects of the mutation of genes for H2O2-scavenging enzymes on the recovery of photosystem II. Pulse labeling experiments revealed that ROS inhibited the synthesis of proteins de novo. In particular, ROS inhibited synthesis of the D1 protein, a component of the reaction center of photosystem II. Northern and western blot analyses suggested that ROS might influence the outcome of photodamage primarily via inhibition of translation of the psbA gene, which encodes the precursor to D1 protein.
  OXFORD UNIV PRESS, English, Scientific journal
  DOI：https://doi.org/10.1093/emboj/20.20.5587
  DOI ID：10.1093/emboj/20.20.5587, ISSN：0261-4189, CiNii Articles ID：80015196667, PubMed ID：11598002, Web of Science ID：WOS:000171766300005
• Bioenergetic responses of Synechocystis 6803 fatty acid desaturase mutants at low temperatures　　　　　　　　　　　　　　　
  R. A. Dilley; Y. Nishiyama; Z. Gombos; N. Murata
  Journal of Bioenergetics and Biomembranes, Volume：33, Number：2, First page：135, Last page：141, 2001, [Reviewed]
  Fatty acid composition of the membrane lipids in the mesophilic cyanobacterium Synechocystis sp. PCC 6803 was altered in earlier work by targeted mutagenesis of genes for fatty acid desaturases. In this work, cells of several mutant strains, depleted in the unsaturated fatty acids in membrane lipids, were grown at 34°C. Spheroplasts (permeabilized cells) were prepared by lysozyme digestion of the cell wall followed by gentle osmotic shock. The bioenergetic parameters ATP formation, electron transport, and H+ uptake were measured at various temperatures. All three bioenergetic parameters for spheroplasts from wild-type cells (which had abundant polyunsaturated fatty acids) were active down to the lowest temperatures used (1°-2°C). In two strains, which lacked the capacity to desaturate fatty acids at the Δ12 position and at the Δ12 and Δ6 positions (designated as desA- and desA-/desD-, respectively), the spheroplasts lost the capacity to form ATP (measured as phenazine methosulfate cyclic phosphorylation) at about 5°C but retained electron transport (water oxidation-dependent ferricyanide reduction) and H+ uptake linked to phenazine methosulfate cyclic electron transport. It appears that the absence of the unsaturation of fatty acids in the Δ12 and Δ6 positions blocks the ability of the photosynthetic membranes to couple a bioenergetically competent proton-motive force to the ATP formation mechanism at temperatures below 5°C. It remains to be determined whether the loss of ATP formation in the mutant strains is the failure of available protons to properly flow into the CF0CF1-ATP synthase or a failure in the CF1 part of the complex in coupling the dissipative H+ flow to the enzyme mechanism of the synthase.
  English, Scientific journal
  DOI：https://doi.org/10.1023/A:1010752531909
  DOI ID：10.1023/A:1010752531909, ISSN：0145-479X, PubMed ID：11456219, SCOPUS ID：0035020641
• Membrane dynamics as seen by Fourier transform infrared spectroscopy in a cyanobacterium, Synechocystis PCC 6803 - The effects of lipid unsaturation and the protein-to-lipid ratio　　　　　　　　　　　　　　　
  B Szalontai; Y Nishiyama; Z Gombos; N Murata
  BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, Volume：1509, Number：1-2, First page：409, Last page：419, Dec. 2000, [Reviewed]
  The roles of lipid unsaturation and lipid-protein interactions in maintaining the physiologically required membrane dynamics were investigated in a cyanobacterium strain, Synechocystis PCC 6803. The specific effects of lipid unsaturation on the membrane structure were addressed by the use of desaturase-deficient (desA(-)/desD(-)) mutant cells (which contain only oleic acid as unsaturated fatty acid species) of Synechocystis PCC 6803. The dynamic properties of the membranes were determined from the temperature dependence of the symmetric CH2 stretching vibration frequency, which is indicative of the lipid fatty acyl chain disorder. It was found that a similar membrane dynamics is maintained at any growth temperature, in both the wild-type and the mutant cell membranes, with the exception of mutant cells grown at the lower physiological temperature limit. It seems that in the physiological temperature range the desaturase system of the cells can modulate the level of lipid desaturation sufficiently to maintain similar membrane dynamics. Below the range of normal growth temperatures, however, the extent of lipid disorder was always higher in the thylakoid than in the cytoplasmic membranes prepared from the same cells. This difference was attributed to the considerable difference in protein-to-lipid ratio in the two kinds of membranes, as determined from the ratio of the intensities of the protein amide I band and the lipid ester C=O vibration. The contributions to the membrane dynamics of an ab ovo present 'structural' lipid disorder due to the protein-lipid interactions and of a thermally induced 'dynamic' lipid disorder could be distinguished. (C) 2000 Elsevier Science B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English, Scientific journal
  DOI：https://doi.org/10.1016/S0005-2736(00)00323-0
  DOI ID：10.1016/S0005-2736(00)00323-0, ISSN：0005-2736, Web of Science ID：WOS:000166177900038
• Acclimation of the photosynthetic machinery to high temperature in Chlamydomonas reinhardtii requires synthesis de novo of proteins encoded by the nuclear and chloroplast genomes　　　　　　　　　　　　　　　
  Y Tanaka; Y Nishiyama; N Murata
  PLANT PHYSIOLOGY, Volume：124, Number：1, First page：441, Last page：449, Sep. 2000, [Reviewed]
  The mechanism responsible for the enhancement of the thermal stability of the oxygen-evolving machinery of photosystem II during acclimation of Chlamydomonas reinhardtii to high temperatures such as 35 degrees C remains unknown. When cells that had been grown at 20 degrees C were transferred to 35 degrees C, the thermal stability of the oxygen-evolving machinery increased and within 8 h it was equivalent to that in cells grown initially at 35 degrees C. Such enhancement of thermal stability was prevented by cycloheximide and by lincomycin, suggesting that the synthesis de novo of proteins encoded by both the nuclear and the chloroplast genome was required for this process. No increase in thermal stability was observed when cells that had been grown at 35 degrees C were exposed to heat shock at 41 degrees C, optimum conditions for the induction of the synthesis of homologs of three heat shock proteins (Hsps), namely, Hsp60, Hsp70, and Hsp22. Moreover, no synthesis of these homologs of Hsps was induced at 35 degrees C. Thus it appears likely that Hsps are not involved in the enhancement of the thermal stability of the oxygen-evolving machinery.
  AMER SOC PLANT BIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.124.1.441
  DOI ID：10.1104/pp.124.1.441, ISSN：0032-0889, eISSN：1532-2548, CiNii Articles ID：80011930242, PubMed ID：10982457, Web of Science ID：WOS:000089306200043
• Ionic and osmotic effects of NaCl-induced inactivation of photosystems I and II in Synechococcus sp.　　　　　　　　　　　　　　　
  SI Allakhverdiev; A Sakamoto; Y Nishiyama; M Inaba; N Murata
  PLANT PHYSIOLOGY, Volume：123, Number：3, First page：1047, Last page：1056, Jul. 2000, [Reviewed]
  We report here that osmotic effects and ionic effects are both involved in the NaCl-induced inactivation of the photosynthetic machinery in the cyanobacterium Synechococcus sp. PCC 7942. Incubation of the cyanobacterial cells in 0.5 M NaCl induced a rapid and reversible decline and subsequent slow and irreversible loss of the oxygen-evolving activity of photosystem (PS) II and the electron transport activity of PSI. An Na+-channel blocker protected both PSII and PSI against the slow, but not the rapid, inactivation. The rapid decline resembled the effect of 1.0 M sorbitol. The presence of both an Na+-channel blocker and a water-channel blocker protected PSI and PSII against the short- and long-term effects of NaCl. Salt stress also decreased cytoplasmic volume and this effect was enhanced by the Na+-channel blocker. Our observations suggested that NaCl had both osmotic and ionic effects. The osmotic effect decreased the amount of water in the cytosol, rapidly increasing the intracellular concentration of salts. The ionic effect was caused by an influx of Na+ ions through potassium/Na+ channels that also increased concentrations of salts in the cytosol and irreversibly inactivated PSI and PSII.
  AMER SOC PLANT PHYSIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.123.3.1047
  DOI ID：10.1104/pp.123.3.1047, ISSN：0032-0889, CiNii Articles ID：80011844163, PubMed ID：10889254, Web of Science ID：WOS:000088213300028
• Inactivation of photosystems I and II in response to osmotic stress in Synechococcus. Contribution of water channels　　　　　　　　　　　　　　　
  SI Allakhverdiev; A Sakamoto; Y Nishiyama; N Murata
  PLANT PHYSIOLOGY, Volume：122, Number：4, First page：1201, Last page：1208, Apr. 2000, [Reviewed]
  The effects of osmotic stress due to sorbitol on the photosynthetic machinery were investigated in the cyanobacterium Synechococcus R-2. Incubation of cells in 1.0 M sorbitol inactivated photosystems I and II and decreased the intracellular solute space by 50%. These effects of sorbitol were reversible: Photosynthetic activity and cytoplasmic volume returned to the original values after removal of the osmotic stress. A blocker of water channels prevented the osmotic-stress-induced inactivation and shrinkage of the intracellular space. It also prevented the recovery of photosynthetic activity and cytoplasmic volume when applied just before release from osmotic stress. Inhibition of protein synthesis by lincomycin had no significant effects on the inactivation and recovery processes, an observation that suggests that protein synthesis was not involved in these processes. Our results suggest that osmotic stress decreased the amount of water in the cytoplasm via the efflux of water through water channels (aquaporins), with resultant increases in intracellular concentrations of ions and a decrease in photosynthetic activity.
  AMER SOC PLANT PHYSIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.122.4.1201
  DOI ID：10.1104/pp.122.4.1201, ISSN：0032-0889, Web of Science ID：WOS:000086903400023
• Genetic engineering of the unsaturation of fatty acids in membrane lipids alters the tolerance of Synechocystis to salt stress　　　　　　　　　　　　　　　
  SI Allakhverdiev; Y Nishiyama; Suzuki, I; Y Tasaka; N Murata
  PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Volume：96, Number：10, First page：5862, Last page：5867, May 1999, [Reviewed]
  The role of unsaturated fatty acids in membrane lipids in the tolerance of the photosynthetic machinery to salt stress was studied by comparing the desA(-)/desD(-) mutant of Synechocystis sp, PCC 6803, which contained monounsaturated fatty acids, with the wild-type strain, which contained a full complement of polyunsaturated fatty acids. In darkness, the loss of oxygen-evolving photosystem II activity in the presence of 0.5 hi NaCl or 0.5 M LiCl was much more rapid in desA(-)/desD(-) cells than in wild-type cells. Oxygen-evolving activity that had been lost during incubation with 0.5 M NaCl in darkness returned when cells were transferred to conditions that allowed photosynthesis or respiration. Recovery was much greater in wild-type than in desA(-)/desD(-) cells, and it was prevented by lincomycin, Thus, the unsaturation of fatty acids is important in the tolerance of the photosynthetic machinery to salt stress. It appears also that the activity and synthesis of the Na+/H+ antiporter system might be suppressed under high-salt conditions and that this effect can be reversed, in part, by the unsaturation of fatty acids in membrane lipids.
  NATL ACAD SCIENCES, English, Scientific journal
  DOI：https://doi.org/10.1073/pnas.96.10.5862
  DOI ID：10.1073/pnas.96.10.5862, ISSN：0027-8424, CiNii Articles ID：80011177011, PubMed ID：10318975, Web of Science ID：WOS:000080246500097
• PsbU, a protein associated with photosystem II, is required for the acquisition of cellular thermotolerance in Synechococcus species PCC 7002　　　　　　　　　　　　　　　
  Y Nishiyama; DA Los; N Murata
  PLANT PHYSIOLOGY, Volume：120, Number：1, First page：301, Last page：308, May 1999, [Reviewed]
  PsbU is an extrinsic protein of the photosystem II complex of cyanobacteria and red algae. Our previous in vitro studies (Y. Nishiyama, D.A. Los, H. Hayashi, N. Murata [1997] Plant Physiol 115: 1473-1480) revealed that PsbU stabilizes the oxygen-evolving machinery of the photosystem II complex against heat-induced inactivation in the cyanobacterium Synechococcus sp. PCC 7002. To elucidate the role of PsbU in vivo, we inactivated the psbU gene in Synechococcus sp. PCC 7002 by targeted mutagenesis. Inactivation of the psbU gene resulted in marked changes in the acclimative responses of cells to high temperature: Mutated cells were unable to increase the thermal stability of their oxygen-evolving machinery when grown at moderately high temperatures. Moreover, the cellular thermotolerance of the mutated cells failed to increase upon acclimation of cells to high temperature. The heat-shock response, as assessed in terms of the levels of homologs of the heat-shock proteins Hsp60, Hsp70, and Hsp17, was unaffected by the mutation in psbU, suggesting that heat-shock proteins were not involved in the changes in the acclimative responses. Our observations indicate that PsbU is involved in the mechanism that underlies the enhancement of the thermal stability of the oxygen-evolving machinery and that the stabilization of the oxygen-evolving machinery is crucial for the acquisition of cellular thermotolerance.
  AMER SOC PLANT PHYSIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.120.1.301
  DOI ID：10.1104/pp.120.1.301, ISSN：0032-0889, CiNii Articles ID：30019360506, PubMed ID：10318707, Web of Science ID：WOS:000080329200031
• Membrane dynamics studied by FTIR spectroscopy in thylakoid and cytoplasmic membranes of Synechocystis PCC6803. Lipids and the effect of protein to lipid ratios　　　　　　　　　　　　　　　
  B Szalontai; Y Nishiyama; Z Gombos; N Murata
  SPECTROSCOPY OF BIOLOGICAL MOLECULES: NEW DIRECTIONS, First page：385, Last page：386, 1999, [Reviewed]
  SPRINGER, English, International conference proceedings
  Web of Science ID：WOS:000085690800172
• Molecular characterization of the PEND protein, a novel bZIP protein present in the envelope membrane that is the site of nucleoid replication in developing plastids　　　　　　　　　　　　　　　
  N Sato; K Ohshima; A Watanabe; N Ohta; Y Nishiyama; J Joyard; R Douce
  PLANT CELL, Volume：10, Number：5, First page：859, Last page：872, May 1998, [Reviewed]
  Plastid nucleoids are known to bind to the envelope membrane in developing chloroplasts. Here, plastid DNA is extensively replicated. We previously detected a DNA binding protein in the inner envelope membranes of developing plastids in pea and named it PEND (for plastid envelope DNA binding) protein. In this study, we report on the structure and molecular characterization of a cDNA for the PEND protein. As a result of screening cDNA libraries in lambda gt11 with one of the target sequences of the PEND protein as a probe, we obtained a clone (PD2) for a novel DNA binding protein consisting of 633 amino acid residues. Analysis of the N-terminal sequence of the purified PEND protein indicated that the transit peptide is just 16 residues long. The PEND protein was detected specifically in the plastid envelope membrane of young unopened leaf buds by immunoblot analysis. The PEND protein consists of a basic region plus zipper region, an unprecedented sextuple repeat region, and a putative membrane-spanning region. The basic region with a zipper region seems to have diverged from that of other plant transcription factors. In addition, the PEND protein could be a distant homolog of the trans-Golgi network integral membrane proteins, The PEND protein is therefore a novel type of DNA binding protein that binds to the membrane as an intrinsic membrane protein.
  AMER SOC PLANT BIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1105/tpc.10.5.859
  DOI ID：10.1105/tpc.10.5.859, ISSN：1040-4651, eISSN：1532-298X, CiNii Articles ID：80010349172, PubMed ID：9596643, Web of Science ID：WOS:000073837400021
• Fatty acids unsaturation of membrane lipids is involved in the tolerance to salt stress　　　　　　　　　　　　　　　
  SI Allakhverdiev; Y Nishiyama; Suzuki, I; Y Tasaka; N Murata
  PHOTOSYNTHESIS: MECHANISMS AND EFFECTS, VOLS I-V, First page：1815, Last page：1818, 1998, [Reviewed]
  SPRINGER, English, International conference proceedings
  Web of Science ID：WOS:000085848500424
• Molecular mechanisms of the low-temperature tolerance of the photosynthetic machinery　　　　　　　　　　　　　　　
  Murata N; Nishiyama Y
  Stress Responses of Photosynthetic Organisms, First page：93, Last page：112, 1998, [Reviewed]
  DOI：https://doi.org/10.1016/C2009-0-00523-6
  DOI ID：10.1016/C2009-0-00523-6
• Role of psbU, an extrinsic protein of photosystem II, in the acquisition of thermotolerance in Synechococcus sp PCC 7002　　　　　　　　　　　　　　　
  Y Nishiyama; DA Los; N Murata
  PHOTOSYNTHESIS: MECHANISMS AND EFFECTS, VOLS I-V, Volume：4, First page：2449, Last page：2452, 1998, [Reviewed]
  SPRINGER, English, International conference proceedings
  DOI：https://doi.org/10.1007/978-94-011-3953-3_573
  DOI ID：10.1007/978-94-011-3953-3_573, Web of Science ID：WOS:000085848500573
• Thermal protection of the oxygen-evolving machinery by PsbU, an extrinsic protein of photosystem II, in Synechococcus species PCC 7002　　　　　　　　　　　　　　　
  Y Nishiyama; DA Los; H Hayashi; N Murata
  PLANT PHYSIOLOGY, Volume：115, Number：4, First page：1473, Last page：1480, Dec. 1997, [Reviewed]
  The evolution of oxygen is the reaction that is the most susceptible to heat in photosynthesis. We showed previously that, in the cyanobacterium Synechococcus sp. PCC 7002, some protein factors located on the thylakoid membranes are involved in the stabilization of this reaction against heat-induced inactivation, and we identified cytochrome c(550) as one such factor (Y. Nishiyama, H. Hayashi, T. Watanabe, N. Murata [1994] Plant Physiol 105: 1313-1319). In the present study we purified another protein that appears to be essential for the stabilization of the oxygen-evolving machinery. The purified protein had an apparent molecular mass of 13 kD, and the gene encoding the 13-kD protein was cloned from Synechococcus sp. PCC 7002 and sequenced. The deduced amino acid sequence revealed that the protein was homologous to PsbU, an extrinsic protein of the photosystem II complex, which has been found in thermophilic species of cyanobacteria. Western analysis showed that the level of PsbU in thylakoid membranes was constant, regardless of the growth temperature. Our studies indicate that PsbU, a constituent of the photosystem II complex, protects the oxygen-evolving machinery against heat-induced inactivation.
  AMER SOC PLANT PHYSIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.115.4.1473
  DOI ID：10.1104/pp.115.4.1473, ISSN：0032-0889, CiNii Articles ID：30019358859, PubMed ID：9414557, Web of Science ID：WOS:000071040500019
• Identification of a cold-regulated RNA-binding protein from the marine cyanobacterium Synechococcus sp. PCC7002　　　　　　　　　　　　　　　
  N Sato; K Maruyama; Y Nishiyama; N Murata
  JOURNAL OF PLANT RESEARCH, Volume：110, Number：1100, First page：405, Last page：410, Dec. 1997, [Reviewed]
  The rbpA gene of a marine cyanobacterium Synechococcus sp. PCC7002 encodes an RNA-binding protein, which exhibited an affinity to poly (G) and poly (U) but not to poly (A) and poly (C). Although there are at least two homologous genes in this cyanobacterium, the RbpA protein was the only RNA-binding protein that was defected in the cell of this strain. This protein was apparently absent in the cells grown at 38 C but was abundant in the cells grown at 25 C.
  BOTANICAL SOC JAPAN, English, Scientific journal
  DOI：https://doi.org/10.1007/BF02506799
  DOI ID：10.1007/BF02506799, ISSN：0918-9440, Web of Science ID：WOS:000071341600003
• The action in vivo of glycine betaine in enhancement of tolerance of Synechococcus sp strain PCC 7942 to low temperature　　　　　　　　　　　　　　　
  P Deshnium; Z Gombos; Y Nishiyama; N Murata
  JOURNAL OF BACTERIOLOGY, Volume：179, Number：2, First page：339, Last page：344, Jan. 1997, [Reviewed]
  The cyanobacterium Synechococcus sp. strain PCC 7942 was transformed with the codA gene for choline oxidase from Arthrobacter globiformis under the control of a constitutive promoter. This transformation allowed the cyanobacterial cells to accumulate glycine betaine at 60 to 80 mM in the cytoplasm, The transformed cells could grow at 20 degrees C, the temperature at which the growth of control cells was markedly suppressed, Photosynthesis of the transformed cells at 20 degrees C was more tolerant to light than that of the control cells, This was caused by the enhanced ability of the photosynthetic machinery in the transformed cells to recover from low-temperature photoinhibition. In darkness, photosynthesis of the transformed cells was more tolerant to low temperature such as 0 to 10 degrees C than that of the control cells, In parallel with the improvement in the ability of the transformed cells to tolerate low temperature, the lipid phase transition of plasma membranes from the liquid-crystalline state to the gel state shifted toward lower temperatures, although the level of unsaturation of the membrane lipids was unaffected by the transformation. These findings suggest that glycine betaine enhances the tolerance of photosynthesis to low temperature.
  AMER SOC MICROBIOLOGY, English, Scientific journal
  DOI：https://doi.org/10.1128/jb.179.2.339-344
  DOI ID：10.1128/jb.179.2.339-344, ISSN：0021-9193, Web of Science ID：WOS:A1997WC27900006
• Targeted mutagenesis of acyl-lipid desaturases in Synechocystis: Evidence for the important roles of polyunsaturated membrane lipids in growth, respiration and photosynthesis　　　　　　　　　　　　　　　
  Y Tasaka; Z Gombos; Y Nishiyama; P Mohanty; T Ohba; K Ohki; N Murata
  EMBO JOURNAL, Volume：15, Number：23, First page：6416, Last page：6425, Dec. 1996, [Reviewed]
  Acyl-lipid desaturases introduce double bonds (unsaturated bonds) at specifically defined positions in fatty acids that are esterified to the glycerol backbone of membrane glycerolipids. The desA, desB and desD genes of Synechocystis sp. PCC 6803 encode acyl-lipid desaturases that introduce double bonds at the Delta 12, omega 3 and Delta 6 positions of C-18 fatty acids respectively. The mutation of each of these genes by insertion of an antibiotic resistance gene cartridge completely eliminated the corresponding desaturation reaction. This system allowed us to manipulate the number of unsaturated bonds in membrane glycerolipids in this organism in a step-wise manner. Comparisons of the variously mutated cells revealed that the replacement of all polyunsaturated fatty acids by a monounsaturated fatty acid suppressed growth of the cells at low temperature and, moreover, it decreased the tolerance of the cells to photoinhibition of photosynthesis at low temperature by suppressing recovery of the photosystem II protein complex from photoinhibitory damage, However, the replacement of tri- and tetraunsaturated fatty acids by a diunsaturated fatty acid did not have such effects, These findings indicate that polyunsaturated fatty acids are important in protecting the photosynthetic machinery from photoinhibition at low temperatures.
  NATURE PUBLISHING GROUP, English, Scientific journal
  ISSN：0261-4189, Web of Science ID：WOS:A1996VZ40900007
• PHOTOSYNTHETIC OXYGEN EVOLUTION IS STABILIZED BY CYTOCHROME C(550) AGAINST HEAT INACTIVATION IN SYNECHOCOCCUS SP PCC-7002　　　　　　　　　　　　　　　
  Y NISHIYAMA; H HAYASHI; T WATANABE; N MURATA
  PLANT PHYSIOLOGY, Volume：105, Number：4, First page：1313, Last page：1319, Aug. 1994, [Reviewed]
  We investigated the factors responsible for the heat stability of photosynthetic oxygen evolution by examining thylakoid membranes from the cyanobacterium Synechococcus sp. PCC 7002. We found that treatment of the thylakoid membranes with 0.1% Triton X-100 resulted in a remarkable decrease in the heat stability of oxygen evolution, and that the heat stability could be restored by reconstituting the membranes with the components that had been extracted by Triton X-100. The protein responsible for the restoration of heat stability was purified from the Triton X-100 extract by two successive steps of chromatography. The purified protein had a molecular mass of 16 kD and exhibited the spectrophotometric properties of a c-type Cyt with a low redox potential. The dithionite-minus-ascorbate difference spectrum revealed an alpha band maximum at 551 nm. We were able to clone and sequence the gene encoding this Cyt from Synechococcus sp. PCC 7002, based on the partial amino-terminal amino acid sequence. The deduced amino acid sequence revealed a gene product consisting of a 34-residue transit peptide and a mature protein of 136 residues. The mature protein is homologous to Cyt c(550), a Cyt with a low redox potential. Thus, our results indicate that Cyt c(550) greatly affects the heat stability of oxygen evolution.
  AMER SOC PLANT PHYSIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1104/pp.105.4.1313
  DOI ID：10.1104/pp.105.4.1313, ISSN：0032-0889, CiNii Articles ID：30019360753, PubMed ID：7972498, Web of Science ID：WOS:A1994PC56800036
• Genetically engineered modification of plant chilling sensitivity and characterization of cyanobacterial heat shock proteins　　　　　　　　　　　　　　　
  H HAYASHI; NISHIDA, I; O ISHIZAKINISHIZAWA; Y NISHIYAMA; N MURATA
  BIOCHEMICAL AND CELLULAR MECHANISMS OF STRESS TOLERANCE IN PLANTS, Volume：86, First page：543, Last page：555, 1994, [Reviewed]
  SPRINGER-VERLAG BERLIN, English, International conference proceedings
  ISSN：1010-8793, Web of Science ID：WOS:A1994BD56F00033
• PURIFICATION AND SUBSTRATE-SPECIFICITY OF CHLOROPHYLLASE FROM CHLORELLA-REGULARIS　　　　　　　　　　　　　　　
  Y NISHIYAMA; M KITAMURA; S TAMURA; T WATANABE
  CHEMISTRY LETTERS, Volume：23, Number：1, First page：69, Last page：72, Jan. 1994, [Reviewed]
  Chlorophyllase was purified 13300-fold from a crude butanol extract of Chlorella regularis. The enzyme clearly recognizes the C13(2) stereochemistry of chlorophyllous pigments in that it hydrolyzes the a and b (13(2)R) forms but not the a' and b' (13(2)S) forms. No enzyme was detected in vivo that specifically hydrolyzes chlorophyll a'.
  CHEMICAL SOC JAPAN, English, Scientific journal
  DOI：https://doi.org/10.1246/cl.1994.69
  DOI ID：10.1246/cl.1994.69, ISSN：0366-7022, eISSN：1348-0715, CiNii Articles ID：10006887931, Web of Science ID：WOS:A1994MV93200021
• PHOTOSYNTHETIC ADAPTATION TO HIGH-TEMPERATURE ASSOCIATED WITH THYLAKOID MEMBRANES OF SYNECHOCOCCUS-PCC7002　　　　　　　　　　　　　　　
  Y NISHIYAMA; E KOVACS; CB LEE; H HAYASHI; T WATANABE; N MURATA
  PLANT AND CELL PHYSIOLOGY, Volume：34, Number：2, First page：337, Last page：343, Mar. 1993, [Reviewed]
  Photosynthetic adaptation to high temperature was investigated in intact cells and isolated thylakoid membranes of the cyanobacterium, Synechococcus PCC7002. In intact cells, the thermal stability of photosynthesis and photosystem 2-mediated electron transport from H2O to 1,4-benzoquinone changed in concert with growth temperature. The photosystem 2-mediated electron transport from H2O to phenyl-1,4-benzoquinone showed greater thermal stability in thylakoid membranes isolated from cells which had adapted to high temperature than in those from non-adapted cells. Enhanced thermal stability was also observed in the thylakoid membranes in the transport of electrons from H2O to 2,6-dichlorophenolindophenol but not in the transport of electrons from diphenylcarbazide to 2,6-dichlorophenolindophenol. These observations suggest that oxygen-evolving sites acquire enhanced thermal stability, and that factors which are responsible for thermal stability remain in isolated thylakoid membranes.
  JAPANESE SOC PLANT PHYSIOLOGISTS, English, Scientific journal
  DOI：https://doi.org/10.1093/oxfordjournals.pcp.a078425
  DOI ID：10.1093/oxfordjournals.pcp.a078425, ISSN：0032-0781, Web of Science ID：WOS:A1993KU14900021
• The adaptation of photosynthesis to high temperature in Synechococcus PCC7002. In Research in Photosynthesis　　　　　　　　　　　　　　　
  Nishiyama Y; Kovács E; Hayashi H; Watanabe T; Murata N
  Research in Photosynthesis, Volume：4, First page：137, Last page：140, 1992, [Reviewed]
• The molecular basis for the acclimation of photosynthesis toward temperature.　　　　　　　　　　　　　　　
  Murata N; Wada H; Nishida I; Gombos Z; Nishiyama Y; Hayashi H; Sakamoto T; Ishizaki-Nishizawa, O; Higashi S
  Research in Photosynthesis, Volume：4, First page：113, Last page：119, 1992, [Reviewed]
• Inhibition of subtilisin BPN′ by reaction site P1 mutants of Streptomyces subtilisin inhibitor　　　　　　　　　　　　　　　
  Shuichi Kojima; Yoshitaka Nishiyama; Izuml Kumagai; Kin-ichiro Miura
  Journal of Biochemistry, Volume：109, Number：3, First page：377, Last page：382, 1991, [Reviewed]
  It has been shown that the P1 site (the center of the reactive site) of protease inhibitors corresponds to the specificity of the cognate protease, and consequently specificity of Streptomyces subtilisin inhibitor (SSI) can be altered by substitution of a single amino acid at the P1 site. In this paper, to investigate whether similar correlation between inhibitory activity of mutated SSI and substrate preference of protease is observed for subtilisin BPN′, which has broad substrate specificity, a complete set of mutants of SSI at the reaction site P1 (position 73) was constructed by cassette and site-directed mutagenesis and their inhibitory activities toward subtilisin BPN′ were measured. Mutated SSIs which have a polar (Ser, Thr, Gin, Asn), basic (Lys, Arg), or aromatic amino acid (Tyr, Phe, Trp, His), or Ala or Leu, at the P1 site showed almost the same strong inhibitory activity toward subtilisin as the wild type (Met) SSI. However, the inhibitory activity of SSI variants with an acidic (Glu, Asp), or a β-branched aliphatic amino acid (Val, Ile), or Gly or Pro, at P1 was decreased. The values of the inhibitor constant (K1) of mutated SSIs toward subtilisin BPN′ were consistent with the substrate preference of subtilisin BPN′. A linear correlation was observed between log(1/K1) of mutated SSIs and (log(1/Km) of synthetic substrates. These results demonstrate that the inhibitory activities of P1 site mutants of SSI are linearly related to the substrate preference of subtilisin BPN′, and indicate that the binding mode of the inhibitors with the protease may be similar to that of substrates, as in the case of trypsin and chymotrypsin. On the other hand, the Cys73 mutant showed only temporary inhibition after mixing of the SSI and subtilisin BPN′, which may be due to irregular disulfide bridge formation in the SSI molecule. © 1991 by The Journal of Biochemistry.
  Oxford University Press, English, Scientific journal
  DOI：https://doi.org/10.1093/oxfordjournals.jbchem.a123389
  DOI ID：10.1093/oxfordjournals.jbchem.a123389, ISSN：0021-924X, PubMed ID：1908859, SCOPUS ID：0026070580

• 有害赤潮藻類Alexandrium属の光合成に対する温度ストレスの影響　　　　　　　　　　　　　　　
  須賀敦紀; 湯浅光貴; 紫加田知幸; 外丸裕司; 西山佳孝
  Volume：2022, 2022
  J-Global ID：202202254327815792
• 赤潮藻類の光応答　　　　　　　　　　　　　　　
  紫加田知幸; 湯浅光貴; 西山佳孝
  光合成研究, Volume：29, Number：2, First page：147‐155, 31 Aug. 2019
  Japanese
  ISSN：1884-2852, J-Global ID：201902228514630242
• エネルギーを使う、捨てる光合成の再最適化-合成生物工学にむけた未踏研究- 中枢代謝を利用した物質生産と光合成能の改変　　　　　　　　　　　　　　　
  小俣 達男; 高谷 信之; 池田 和貴; 愛知 真木子; 西山 佳孝
  Volume：平成30年度, First page：219, Last page：219, Aug. 2018
  Japanese
  医中誌Web ID：2019221982
• 光合成におけるカロテノイドの機能　　　　　　　　　　　　　　　
  髙橋拓子; 西山佳孝
  Volume：9, First page：50, Last page：62, Aug. 2018, [Reviewed], [Invited]
  Japanese, Introduction scientific journal
• 赤潮藻類Karenia mikimotoiの生残,光合成,遊泳に及ぼす貧栄養と強光の影響　　　　　　　　　　　　　　　
  湯浅光貴; 紫加田知幸; 西山佳孝
  Volume：2018, 2018
  J-Global ID：201802245581035074
• 赤潮藻類Karenia mikimotoiの光合成に及ぼす栄養欠乏と光強度の影響　　　　　　　　　　　　　　　
  湯浅光貴; 紫加田知幸; 西山佳孝
  Volume：2018, 2018
  J-Global ID：201802287711821388
• 光化学系IIの光阻害:光損傷と修復阻害のメカニズム　　　　　　　　　　　　　　　
  西山佳孝
  光合成研究, Volume：23, Number：2, First page：50, Last page：56, Aug. 2013, [Reviewed], [Invited]
  Japanese
  ISSN：1884-2852, J-Global ID：201302211700088397, CiNii Articles ID：40019797444
• The mechanism of photoinhibition in vivo: Re-evaluation of the roles of catalase, alpha-tocopherol, non-photochemical quenching, and electron transport　　　　　　　　　　　　　　　
  Norio Murata; Suleyman I. Allakhverdiev; Yoshitaka Nishiyama
  BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Volume：1817, Number：8, First page：1127, Last page：1133, Aug. 2012
  Photoinhibition of photosystem II (PSII) occurs when the rate of light-induced inactivation (photodamage) of PSII exceeds the rate of repair of the photodamaged PSII. For the quantitative analysis of the mechanism of photoinhibition of PSII, it is essential to monitor the rate of photodamage and the rate of repair separately and, also, to examine the respective effects of various perturbations on the two processes. This strategy has allowed the re-evaluation of the results of previous studies of photoinhibition and has provided insight into the roles of factors and mechanisms that protect PSII from photoinhibition, such as catalases and peroxidases, which are efficient scavengers of H2O2: alpha-tocopherol, which is an efficient scavenger of singlet oxygen: non-photochemical quenching, which dissipates excess light energy that has been absorbed by PSII: and the cyclic and non-cyclic transport of electrons. Early studies of photoinhibition suggested that all of these factors and mechanisms protect PSII against photodamage. However, re-evaluation by the strategy mentioned above has indicated that, rather than protecting PSII from photodamage, they stimulate protein synthesis, with resultant repair of PSII and mitigation of photoinhibition. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: from Natural to Artificial. (C) 2012 Elsevier B.V. All rights reserved.
  ELSEVIER SCIENCE BV, English, Book review
  DOI：https://doi.org/10.1016/j.bbabio.2012.02.020
  DOI ID：10.1016/j.bbabio.2012.02.020, ISSN：0005-2728, Web of Science ID：WOS:000306202700004
• Repair mechanisms of photosynthesis from photodamage　　　　　　　　　　　　　　　
  西山佳孝
  旭硝子財団助成成果報告書(Web), Volume：2012, First page：NO.29 (WEB ONLY), Last page：6, 2012
  Japanese
  ISSN：1882-0069, J-Global ID：201302288140178517, CiNii Articles ID：40019979752
• Expression of bacterial tyrosine ammonia-lyase creates a novel p-coumaric acid pathway in the biosynthesis of phenylpropanoids in Arabidopsis.　　　　　　　　　　　　　　　
  Nishiyama, Y; Yun, C. S; Sasaki, T; Tozawa, Y
  PLANTA, Volume：232, Number：1, First page：209, Last page：218, 2010, [International magazine]
  Some flavonoids are considered as beneficial compounds because they exhibit anticancer or antioxidant activity. In higher plants, flavonoids are secondary metabolites that are derived from phenylpropanoid biosynthetic pathway. A large number of phenylpropanoids are generated from p-coumaric acid, which is a derivative of the primary metabolite, phenylalanine. The first two steps in the phenylpropanoid biosynthetic pathway are catalyzed by phenylalanine ammonia-lyase and cinnamate 4-hydroxylase, and the coupling of these two enzymes forms a rate-limiting step in the pathway. For the generation of p-coumaric acid, the conversion from phenylalanine to p-coumaric acid that is catalyzed by two enzymes can be theoretically performed by a single enzyme, tyrosine ammonia-lyase (TAL) that catalyzes the conversion of tyrosine to p-coumaric acid in certain bacteria. To modify the p-coumaric acid pathway in plants, we isolated a gene encoding TAL from a photosynthetic bacterium, Rhodobacter sphaeroides, and introduced the gene (RsTAL) in Arabidopsis thaliana. Analysis of metabolites revealed that the ectopic over-expression of RsTAL leads to higher accumulation of anthocyanins in transgenic 5-day-old seedlings. On the other hand, 21-day-old seedlings of plants expressing RsTAL showed accumulation of higher amount of quercetin glycosides, sinapoyl and p-coumaroyl derivatives than control. These results indicate that ectopic expression of the RsTAL gene in Arabidopsis enhanced the metabolic flux into the phenylpropanoid pathway and resulted in increased accumulation of flavonoids and phenylpropanoids.
  English
  DOI：https://doi.org/10.1007/s00425-010-1166-1
  DOI ID：10.1007/s00425-010-1166-1, ISSN：0032-0935, CiNii Articles ID：80021069995, PubMed ID：20396902
• ラン藻の光化学系IIの高温適応に関与する脂肪酸合成酵素　　　　　　　　　　　　　　　
  南條洋平; 和田元; 林秀則; 西山佳孝
  日本植物生理学会年会要旨集, Volume：49th, First page：104, 15 Mar. 2008
  Japanese
  DOI：https://doi.org/10.14841/jspp.2008.0.0015.0
  DOI ID：10.14841/jspp.2008.0.0015.0, J-Global ID：200902234956833399
• ダイズ培養細胞のチラコイド膜における光化学系IIの高温適応の分子機構　　　　　　　　　　　　　　　
  武智和也; 南條洋平; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Volume：48th, First page：257, 15 Mar. 2007
  Japanese
  DOI：https://doi.org/10.14841/jspp.2007.0.651.0
  DOI ID：10.14841/jspp.2007.0.651.0, J-Global ID：200902254370911413
• Action of reactive oxygen species in the photoinhibition of photosystem II　　　　　　　　　　　　　　　
  Y. Nishiyama; K. Kojima; H. Hayashi; S. Allakhverdiev; N. Murata
  PHOTOSYNTHESIS RESEARCH, Volume：91, Number：2-3, First page：284, Last page：284, Feb. 2007
  SPRINGER, English, Summary international conference
  ISSN：0166-8595, Web of Science ID：WOS:000248151000572
• Acclimation of photosystem II to high temperature in thylakoid membrane of suspension-cultured cells of soybean　　　　　　　　　　　　　　　
  Kazuya Takechi; Yohei Nanjo; Yoshitaka Nishiyama; Hidenori Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：48, First page：S179, Last page：S179, 2007
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000245922701195
• Regulation of the translational machinery under oxidative stress in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Yoshitaka Nishiyama; Kouji Kojima; Masaru Oshita; Toru Hisabori; Hidenori Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：48, First page：S4, Last page：S4, 2007
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000245922700017
• Effects of oxidative stress on protein synthesis in an in vitro translation system from Synechocystis sp PCC6803　　　　　　　　　　　　　　　
  Kouii Kojima; Masaru Oshita; Hidenori Hayashi; Yoshitaka Nishiyama
  PLANT AND CELL PHYSIOLOGY, Volume：48, First page：S157, Last page：S157, 2007
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000245922701105
• Interaction between elongation factor G and thioredoxin in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Masaru Oshita; Kouji Kojima; Toru Hisabori; Yoshitaka Nishiyama; Hidenori Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：48, First page：S176, Last page：S176, 2007
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000245922701182
• Tolerance of photosynthesis to oxidative stress in cyanobacterial mutants that overexpress antioxidant enzymes　　　　　　　　　　　　　　　
  Ai Nakano; Akiko Noda; Hidetoshi Okuyama; Yoshitaka Nishiyama; Hidenori Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：48, First page：S179, Last page：S179, 2007
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000245922701196
• ダイズ培養細胞における光化学系IIの高温傷害と高温適応　　　　　　　　　　　　　　　
  西山佳孝; 南條洋平; 武智和也; 村田紀夫; 林秀則
  日本植物生理学会年会要旨集, Volume：47th, First page：210, Mar. 2006
  Japanese
  DOI：https://doi.org/10.14841/jspp.2006.0.421.0
  DOI ID：10.14841/jspp.2006.0.421.0, J-Global ID：200902208612366677
• ラン藻の光化学系IIの高温適応に関与するタンパク質の解析　　　　　　　　　　　　　　　
  南條洋平; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Volume：47th, First page：210, Mar. 2006
  Japanese
  DOI：https://doi.org/10.14841/jspp.2006.0.422.0
  DOI ID：10.14841/jspp.2006.0.422.0, J-Global ID：200902299757762061
• Effects of oxidative stress oil the synthesis of the D1 protein in an in vitro translation system from Synechocystis sp strain PCC 6803　　　　　　　　　　　　　　　
  K Kojima; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：47, First page：S129, Last page：S129, 2006
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000236401401002
• Selective accumulation of heavy metal ions with polypeptides including tandemly-connected N-terminal regions of cyanobacterial SmtA　　　　　　　　　　　　　　　
  M Nakaoka; N Matsumoto; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：47, First page：S232, Last page：S232, 2006
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000236401401412
• Response of photosystem II to high temperature in a cell-suspension culture of soybean　　　　　　　　　　　　　　　
  Y Nishiyama; Y Nanjo; K Takechi; N Murata; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：47, First page：S129, Last page：S129, 2006
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000236401401003
• Proteomic analysis of the acclimation of photosystem II to high temperature in Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  Y Nanjo; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：47, First page：S129, Last page：S129, 2006
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000236401401004
• Function and molecular evolution of ADP-ribose pyrophosphatase family in the Synechocystis sp PCC 6803　　　　　　　　　　　　　　　
  K Okuda; Y Koshimi; K Hisataka; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：46, First page：S111, Last page：S111, 2005
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000228104100443
• Metal binding of polypeptides including tandemly-connected N-terminal regions of cyanobacterial SmtA　　　　　　　　　　　　　　　
  H Hayashi; N Matsumoto; M Nakaoka; Y Nishiyama
  PLANT AND CELL PHYSIOLOGY, Volume：46, First page：S58, Last page：S58, 2005
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000228104100231
• 環境ストレスと光合成の修復　　　　　　　　　　　　　　　
  西山佳孝
  Volume：39, First page：8, Last page：12, Aug. 2004, [Reviewed]
  Japanese, Introduction scientific journal
• Biochemical and physiological studies of a novel nudix hydrolase, NuhA, in cyanobacteria　　　　　　　　　　　　　　　
  K Okuda; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：45, First page：S101, Last page：S101, 2004
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000220592700400
• Heavy metal resistance of transgenic Arabidopsis carrying the genes for heavy-metal-transporting P-type ATPase of yeast　　　　　　　　　　　　　　　
  E Shiraishi; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：45, First page：S30, Last page：S30, 2004
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000220592700117
• Inhibition of the repair of photosystem II by oxidative stress in Chlamydomonas reinhardtii　　　　　　　　　　　　　　　
  Y Nishiyama; T Kanematsu; N Murata; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：45, First page：S159, Last page：S159, 2004
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000220592700630
• The 2nd Japan-Germany Binational Symposium　　　　　　　　　　　　　　　
  西山佳孝
  Volume：37, First page：18, Last page：20, Dec. 2003, [Reviewed]
  Japanese, Introduction scientific journal
• Nudix hydrolase bound to the heat shock promoter in cyanobacteria　　　　　　　　　　　　　　　
  K Okuda; M Masuyama; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：44, First page：S117, Last page：S117, 2003
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000181914300464
• Different transcriptional repression of metal induced genes in Cyanobacteria　　　　　　　　　　　　　　　
  S Kawamoto; EH Morita; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：44, First page：S200, Last page：S200, 2003
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000181914300794
• In vivo action of singlet oxygen in the repair of photodamage to photosystem II　　　　　　　　　　　　　　　
  Y Nishiyama; SI Allakhverdiev; H Yamamoto; H Hayashi; N Murata
  PLANT AND CELL PHYSIOLOGY, Volume：44, First page：S25, Last page：S25, 2003
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000181914300096
• Analysis of rpoHgene expression in the psychrophilic bacterium, Colwellia maris.　　　　　　　　　　　　　　　
  S Yamauchi; K Miyagi; H Okuyama; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：44, First page：S140, Last page：S140, 2003
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000181914300556
• Reactive oxygen species inhibit the translational machinery in the repair of photosystem II　　　　　　　　　　　　　　　
  Y Nishiyama; H Yamamoto; SI Allakhverdiev; N Murata
  PLANT AND CELL PHYSIOLOGY, Volume：43, First page：S28, Last page：S28, 2002
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000174726400094
• Characterization of a cyanobacterial mutant sensitive to high temperature　　　　　　　　　　　　　　　
  A Kimura; H Morita; H Toh; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：43, First page：S114, Last page：S114, 2002
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000174726400412
• Functional analysis of a protein bound to the heat shock promoter in Synechococcus sp PCC 7002　　　　　　　　　　　　　　　
  K Okuda; H Morita; H Sasaki; Y Nishiyama; H Hayashi
  PLANT AND CELL PHYSIOLOGY, Volume：43, First page：S116, Last page：S116, 2002
  OXFORD UNIV PRESS, English, Summary international conference
  ISSN：0032-0781, Web of Science ID：WOS:000174726400418
• EFFECTS OF REACTIVE OXYGEN SPECIES ON THE PHOTOINHIBITION OF PHOTOSYSTEM II IN Synechocystis SP. PCC 6803 :　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka; YAMAMOTO Hiroshi; YOKOTA Akiho; MURATA Norio
  Plant and cell physiology, Volume：41, First page：s175, 2000
  Japanese Society of Plant Physiologists, English
  ISSN：0032-0781, CiNii Articles ID：110003722553, CiNii Books ID：AA0077511X
• COOPERATION OF NUCLEAR AND CHLOROPLASTIC GENOMES IN THE PHOTOSYNTHETIC ACCLIMATION OF CHLAMYDOMONAS TO HIGH TEMPERATURE :　　　　　　　　　　　　　　　
  TANAKA Yuji; NISHIYAMA Yoshitaka; MURATA Norio
  Plant and cell physiology, Volume：41, First page：s44, 2000
  Japanese Society of Plant Physiologists, English
  ISSN：0032-0781, CiNii Articles ID：110003722100, CiNii Books ID：AA0077511X
• A CHLAMYDOMONAS MUTANT DEFECTIVE IN THE CONVERSION OF VIOLAXANTHIN TO NEOXANTHIN IN ABA BIOSYNTHESIS :　　　　　　　　　　　　　　　
  Katoh Akira; Alia; Chen Tony H. H.; Nishiyama Yoshitaka; Takaichi Shinichi; Ishizaki Kimihiro; Fukuzawa Hideya; Murata Norio
  Plant and cell physiology, Volume：41, First page：s142, 2000
  Japanese Society of Plant Physiologists, English
  ISSN：0032-0781, CiNii Articles ID：110003722442, CiNii Books ID：AA0077511X
• INCREASE IN TOLERANCE OF THE PHOTOSYNTHETIC MACHINERY TO SALT STRESS BY GENETIC ENHANCEMENT OF UNSATURATION OF FATTY ACIDS IN MEMBRANE LIPIDS IN Synechococcus　　　　　　　　　　　　　　　
  ALLAKHVERDIEV Suleyman; SUZUKI Iwane; NISHIYAMA Yoshitaka; INABA Masami; MURATA Norio
  Volume：40, First page：s121, Last page：s121, Mar. 1999
  English
  ISSN：0032-0781, CiNii Articles ID：10003758210, CiNii Books ID：AA0077511X
• PHYSIOLOGICAL IMPLICATION OF THE ACQUISITION OF THERMOTOLERANCE OF THE OXYGEN-EVOLVING MACHINERY IN THE CYANOBACTERIUM, Synechococcus sp. PCC 7002　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka; MURATA Norio
  Volume：39, First page：S34, Last page：S34, May 1998
  English
  ISSN：0032-0781, CiNii Articles ID：10003751600, CiNii Books ID：AA0077511X
• INVOLVEMENT OF A 13-KDA PROTEIN IN STABILIZATION OF OXYGEN EVOLUTION AGAINST HEAT INACTIVATION IN THE CYANOBACTERIUM, Synechococcus sp. PCC 7002　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka; LOS Dmitry A.; HAYASHI Hidenori; MURATA Norio
  Volume：37, First page：31, Last page：31, Mar. 1996
  English
  ISSN：0032-0781, CiNii Articles ID：10002707903, CiNii Books ID：AA0077511X
• IN VIVO ACTION OF GLYCINEBETAINE IN ENHANCING THE TOLERANCE TO HIGH AND LOW TEMPERATURE　　　　　　　　　　　　　　　
  DESHNIUM Patcharaporn; GOMBOS Zoltan; NISHIYAMA Yoshitaka; MURATA Norio
  Volume：37, First page：59, Last page：59, Mar. 1996
  English
  ISSN：0032-0781, CiNii Articles ID：10002708016, CiNii Books ID：AA0077511X
• HOW CYANOBACTERIA ENHANCE THEIR THERMAL TOLERANCE AND ADAPT TO HIGH TEMPERATURE STRESSES?　　　　　　　　　　　　　　　
  HAYASHI H.; NISHIYAMA Y.; MURATA N.
  Volume：70, Number：6, First page：702, Last page：702, 01 Dec. 1995
  English
  ISSN：0021-504X, CiNii Articles ID：10002711825, CiNii Books ID：AA00690924
• THE HEAT TOLERANCE OF PHOTOSYNTHESIS INTHE CYANOBACTERIUM, Synechococcus PCC 7002 AND SOYBEAN CULTUREDCELLS　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka; HAYASHI Hidenori; WATANABE Tadashi; MURATA Norio
  Volume：36, First page：S137, Mar. 1995
  English
  ISSN：0032-0781, CiNii Articles ID：10004344434, CiNii Books ID：AA0077511X
• THE ADAPTATION OF PHOTOSYNTHESIS TO HIGH-TEMPERATURE IN SYNECHOCOCCUS PCC7002　　　　　　　　　　　　　　　
  Y NISHIYAMA; E KOVACS; H HAYASHI; T WATANABE; N MURATA
  PHOTOSYNTHESIS RESEARCH, Volume：34, Number：1, First page：214, Last page：214, Oct. 1992
  KLUWER ACADEMIC PUBL, English, Summary international conference
  ISSN：0166-8595, Web of Science ID：WOS:A1992JV84800626

• 有害赤潮藻Chattonella属の細胞外多糖およびスーパーオキシド産生と魚毒性との関係　　　　　　　　　　　　　　　
  高嶋渓; 湯浅光貴; 紫加田知幸; 小竹敬久; 西山佳孝
  Mar. 2025
  Japanese, Oral presentation
  共同研究・競争的資金等ID：35766110
• 有害赤潮藻Chattonella属の魚毒因子の探索　　　　　　　　　　　　　　　
  湯浅光貴; 高嶋渓; 西山佳孝
  Mar. 2025
  Japanese, Oral presentation
  共同研究・競争的資金等ID：35766110
• 海洋微生物叢におけるメタ脂質代謝動態の解明　　　　　　　　　　　　　　　
  峯村友輝; 湯浅光貴; 戸田成美; 滝沢侑子; 廣田隆一; 力石嘉人; 西山佳孝; 神保晴
  Mar. 2025
  Japanese, Poster presentation
• シアノバクテリアSynechococcus elongatus PCC 7942 の代謝改変による遊離脂肪酸生産　　　　　　　　　　　　　　　
  古島翼; 西本琴羽; 神保晴彦; 山本哲史; 門脇太朗; 高谷信之; 愛知真木子; 池田和貴; 小俣達男; 西山佳
  Mar. 2025
  Japanese, Oral presentation
  共同研究・競争的資金等ID：35751372
• シロイヌナズナの葉における新規油滴局在リパーゼの同定と機能解析　　　　　　　　　　　　　　　
  黒澤優里; 神保晴彦; 西山佳孝; 島田貴士
  Mar. 2025
  Japanese, Poster presentation
• 光化学系IIの高温耐性における抗酸化能およびタンパク質合成の役割　　　　　　　　　　　　　　　
  Pornpan Napaumpaipor; 西山佳孝
  Mar. 2025
  Japanese, Oral presentation
  共同研究・競争的資金等ID：43652948
• 緑藻クラミドモナスにおけるPSI光阻害の解析　　　　　　　　　　　　　　　
  小池壮太郎; 高木咲歩; 浅見侑人; 西山佳孝; 高橋拓子
  Mar. 2025
  Japanese, Oral presentation
  共同研究・競争的資金等ID：45123620
• シアノバクテリアの光化学系における鏡像異性体 PG の影響　　　　　　　　　　　　　　　
  棚瀬元貴; 安部真人; 和田元; 西山佳孝; 神保晴彦
  Mar. 2025
  Japanese, Oral presentation
• 光化学系II修復のレドックス制御と強光耐性　　　　　　　　　　　　　　　
  西山佳孝
  Dec. 2024, [Invited]
  Japanese, Invited oral presentation
  共同研究・競争的資金等ID：43652948
• シアノバクテリアの光化学系IIにおける鏡像異性体PGの影響　　　　　　　　　　　　　　　
  棚瀬元貴; 安部真人; 和田元; 西山佳孝; 神保晴彦
  Dec. 2024
  Japanese, Poster presentation
• シアノバクテリアSynechococcus elongatus PCC 7942を用いた遊離脂肪酸の細胞外生産　　　　　　　　　　　　　　　
  古島翼; 西本琴羽; 山本哲史; 門脇太朗; 愛知真木子; 高谷信之; 池田和貴; 小俣達男; 西山佳孝
  Dec. 2024
  Japanese, Poster presentation
  共同研究・競争的資金等ID：35751372
• 微細藻類を用いたバイオ燃料生産開発　　　　　　　　　　　　　　　
  西山佳孝
  Dec. 2024, [Invited]
  Japanese, Invited oral presentation
  共同研究・競争的資金等ID：35751372
• Redox regulation of the repair of photosystem II via translation factors　　　　　　　　　　　　　　　
  Yoshitaka Nishiyama; Pornpan Napaumpaiporn
  Sep. 2024
  English, Oral presentation
  共同研究・競争的資金等ID：43652948
• シアノバクテリアSynechococcus elongatus PCC 7942の遊離脂肪酸生産株の脂肪酸フラックス解析　　　　　　　　　　　　　　　
  古島翼; 神保晴彦; 西本琴羽; 門脇太朗; 愛知真木子; 高谷信之; 池田和貴; 小俣達男; 西山佳孝
  Sep. 2024
  Japanese, Poster presentation
  共同研究・競争的資金等ID：35751372
• シアノバクテリアを用いた遊離脂肪酸の細胞外生産法の開発　　　　　　　　　　　　　　　
  西山佳孝; 古島翼; 西本琴羽; 山本哲史; 門脇太朗; 愛知真木子; 高谷信之; 池田和貴; 小俣達男
  Sep. 2024
  Japanese, Oral presentation
  共同研究・競争的資金等ID：35751372
• 赤潮形成藻シャットネラ属の光合成環境適応機構　　　　　　　　　　　　　　　
  西山佳孝; 神保晴彦; 湯浅光貴
  Jun. 2024
  Japanese, Oral presentation
• 赤潮藻類の光合成と遊泳運動　　　　　　　　　　　　　　　
  西山佳孝; 小澤竜太; 湯浅光貴; 紫加田知幸
  May 2024, [Invited]
  Japanese, Invited oral presentation
  共同研究・競争的資金等ID：35751341
• Response of photosynthesis to strong light　　　　　　　　　　　　　　　
  Yoshitaka Nishiyama
  May 2024, [Invited]
  English, Invited oral presentation
  共同研究・競争的資金等ID：43652948
• 有害赤潮藻Chattonella marinaの細胞外多糖構造とスーパーオキシド産生機構　　　　　　　　　　　　　　　
  高嶋渓; 湯浅光貴; 紫加田知幸; 小竹敬久; 西山佳孝
  Mar. 2024
  Japanese, Oral presentation
  共同研究・競争的資金等ID：35751341
• 有害赤潮藻類の強光に対する逃避運動　　　　　　　　　　　　　　　
  小澤竜太; 湯浅光貴; 紫加田知幸; 西山佳孝
  Mar. 2024
  Japanese, Poster presentation
  共同研究・競争的資金等ID：35751341
• Enhanced tolerance of photosystem II to strong light and high temperature via reinforcement of translational and antioxidation systems in Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  Pornpan Napaumpaiporn; Takako Ogawa; Kintake Sonoike; Yoshitaka Nishiyama
  Mar. 2024
  English, Oral presentation
• 光化学系IIのTwo-step光損傷機構の再検討　　　　　　　　　　　　　　　
  小島俊太; 西山佳孝
  Mar. 2024
  Japanese, Oral presentation
  共同研究・競争的資金等ID：43652948
• クラミドモナスPGRL1タンパク質におけるシステイン残基の機能解析　　　　　　　　　　　　　　　
  高橋拓子; 井須敦子; 吉田啓亮; 若林憲一; 久堀徹; 西山佳孝
  Mar. 2024
  Japanese, Oral presentation
• シロイヌナズナにおけるNPQ関連遺伝子PSBSの発現制御解析　　　　　　　　　　　　　　　
  櫻井まどか; 八巻遥佳; Krishna K. Niyogi; 西山佳孝; 高橋拓子
  Mar. 2024
  Japanese, Poster presentation
• クロロフィル蛍光定常レベルの光依存性により明らかになったシアノバクテリアのエネルギー散逸機構の特性　　　　　　　　　　　　　　　
  小川敬子; 高橋拓子; 西山佳孝; 日原由香子; 園池公毅
  Mar. 2024
  Japanese, Oral presentation
• シアノバクテリアSynechococcus elongatus PCC 7942におけるリパーゼ過剰発現による遊離脂肪酸生産　　　　　　　　　　　　　　　
  古島翼; 門脇太朗; 松崎雄代; 山本哲史; 高谷信之; 愛知真木子; 池田和貴; 小俣達男; 西山佳孝
  Mar. 2024
  Japanese, Oral presentation
  共同研究・競争的資金等ID：35751372
• 光化学系IIのTwo-step光損傷機構の解析　　　　　　　　　　　　　　　
  小島俊太; 西山佳孝
  Jun. 2023
  Japanese, Poster presentation
  共同研究・競争的資金等ID：43652948
• Improved capacity for the repair of photosystem II under strong light via alteration of antioxidative systems　　　　　　　　　　　　　　　
  Pornpan Napaumpaiporn; Takako Ogawa; Kintake Sonoike; Yoshitaka Nishiyama
  Jun. 2023
  English, Poster presentation
  共同研究・競争的資金等ID：43652948
• 有害赤潮藻類Chattonella属の細胞表層多糖の構造と魚毒性の関係　　　　　　　　　　　　　　　
  田村悠; 湯浅光貴; 紫加田知幸; 小竹敬久; 西山佳孝
  Mar. 2023
• Improved capacity of photosystem II for minimizing photoinhibition via modification of translation and antioxidative systems in Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  Pornpan Napaumpaiporn; Yoshitaka Nishiyama
  Mar. 2023
• 光化学系IIの強光順化におけるカロテノイド配糖体の役割　　　　　　　　　　　　　　　
  恩田萌花; 海發育実; 出原太智; 高市真一; 西山佳孝
  Mar. 2023
• 強力なUV-A照射を用いた光化学系IIの光阻害解析　　　　　　　　　　　　　　　
  小島俊太; 西山佳孝
  Mar. 2023
• クラミドモナスPGRL1がPSI光防御に果たす役割　　　　　　　　　　　　　　　
  高橋拓子; 髙山健太; 井須敦子; 若林憲一; 久堀徹; 西山佳孝
  Mar. 2023
• 有害赤潮藻類における日周鉛直運動と光合成の関係　　　　　　　　　　　　　　　
  西山佳孝
  Mar. 2023, [Invited]
• Effects of reinforced translation and antioxidative systems on photoinhibition of photosystem II in Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  Pornpan Napaumpaiporn; Yoshitaka Nishiyama
  Dec. 2022
• 光化学系IIの強光耐性におけるカロテノイド配糖体の役割　　　　　　　　　　　　　　　
  恩田萌花; 海發育実; 出原太智; 高市真一; 西山佳孝
  Dec. 2022
• 強力なUV-A照射による光化学系II光阻害機構の解析　　　　　　　　　　　　　　　
  小島俊太; 西山佳孝
  Dec. 2022
• 光合成微生物シアノバクテリアを用いたバイオ燃料生産　　　　　　　　　　　　　　　
  西山佳孝
  Oct. 2022, [Invited]
• 強力なUV-A照射を用いた光化学系IIの光損傷機構の解析　　　　　　　　　　　　　　　
  小島俊太; 西山佳孝
  May 2022
• 有害赤潮藻類Chattonella属の細胞表層グリコカリックスの糖鎖分析　　　　　　　　　　　　　　　
  田村悠; 湯浅光貴; 紫加田知幸; 西山佳孝
  Mar. 2022
• 有害赤潮藻類Alexandrium属の光合成に対する温度ストレスの影響　　　　　　　　　　　　　　　
  須賀敦紀; 湯浅光貴; 紫加田知幸; 西山佳孝
  Mar. 2022
• シアノバクテリアSynechocystis sp. PCC 6803が持つ2型ジアシルグリセロールアシルトランスフェラーゼホモログ遺伝子　　　　　　　　　　　　　　　
  平井一帆; 青木元秀; 西山佳孝; 都筑幹夫; 佐藤典弘
  Mar. 2022
• 高温順化したシアノバクテリアの光阻害における光化学系II表在性タンパク質の役割　　　　　　　　　　　　　　　
  猪崎風葉; 西山佳孝
  Mar. 2022
• シロイヌナズナの強光順化における葉序ごとの光化学系II修復能力　　　　　　　　　　　　　　　
  北村泉希; 新庄梓; 西山佳孝
  Mar. 2022
• Eco-physiological study of noxious red-tide-forming microalgae　　　　　　　　　　　　　　　
  Koki Yuasa; Tomoyuki Shikata; Yoshitaka Nishiyama
  Mar. 2022, [Invited]
• 光化学系IIの光阻害と修復の分子機構　　　　　　　　　　　　　　　
  小島俊太; 西山佳孝
  Mar. 2022
• 有害赤潮ラフィド藻Chattonella antiquaの魚毒性に及ぼす栄養欠乏の影響　　　　　　　　　　　　　　　
  湯浅光貴; 紫加田知幸; 田村悠; 小竹敬久; 西山佳孝
  Sep. 2021
  Sep. 2021 - Sep. 2021
• 光化学系IIの光阻害と修復の分子機構　　　　　　　　　　　　　　　
  小島俊太; 西山佳孝
  Aug. 2021
  Aug. 2021 - Aug. 2021, Japanese, Poster presentation
  共同研究・競争的資金等ID：35751334
• Role of the chloroplast translation factor EF-Tu in photoinhibition of photosystem II in Arabidopsis　　　　　　　　　　　　　　　
  Yoshitaka Nishiyama
  Aug. 2021, [Invited]
  Aug. 2021 - Aug. 2021, English, Invited oral presentation
  共同研究・競争的資金等ID：12898660
• シアノバクテリアの強光順化におけるカロテノイド配糖体の役割　　　　　　　　　　　　　　　
  恩田萌花; 海發育実; 出原太智; 高市真一; 西山佳孝
  May 2021
  May 2021 - May 2021, Japanese, Oral presentation
  共同研究・競争的資金等ID：12898660
• 光化学系IIの修復におけるカルシウムイオンの役割　　　　　　　　　　　　　　　
  猪崎風葉; 西山佳孝
  May 2021
  May 2021 - May 2021, Japanese, Oral presentation
  共同研究・競争的資金等ID：35751334
• 有害赤潮藻Chattonella antiquaの活性酸素産生に及ぼす栄養欠乏の影響　　　　　　　　　　　　　　　
  湯浅光貴; 市川隆祥; 田村悠; 紫加田知幸; 西山佳孝
  Mar. 2021
  Mar. 2021 - Mar. 2021, Japanese, Oral presentation
  共同研究・競争的資金等ID：35766110
• 新奇有害赤潮藻Alexandrium leeiの増殖と光合成に対する温度ストレスの影響　　　　　　　　　　　　　　　
  須賀敦紀; 湯浅光貴; 紫加田知幸; 西山佳孝
  Mar. 2021
  Mar. 2021 - Mar. 2021, Japanese, Oral presentation
  共同研究・競争的資金等ID：35766110
• 有害赤潮藻Chattonella属におけるスーパーオキシド産生機構の生化学解析　　　　　　　　　　　　　　　
  市川隆祥; 湯浅光貴; 紫加田知幸; 西山佳孝
  Mar. 2021
  Mar. 2021 - Mar. 2021, Japanese, Oral presentation
  共同研究・競争的資金等ID：35766110
• 有害赤潮形成藻Chattonella antiquaの細胞外スーパーオキシド産生を促進する環境要因　　　　　　　　　　　　　　　
  湯浅光貴; 市川隆祥; 田村悠; 紫加田知幸; 西山佳孝
  Mar. 2021
  Mar. 2021 - Mar. 2021, Japanese, Oral presentation
  共同研究・競争的資金等ID：35766110
• クラミドモナスPGRL1システイン残基の機能解析　　　　　　　　　　　　　　　
  高橋拓子; 髙山健太; 井須敦子; 若林憲一; 久堀徹; 西山佳孝
  Mar. 2021
  Mar. 2021 - Mar. 2021, Japanese, Oral presentation
• シロイヌナズナ葉緑体翻訳因子EF-Tuの酸化傷害と光化学系IIの光阻害の関係　　　　　　　　　　　　　　　
  鳥生万智; 新庄梓; 西山佳孝
  Mar. 2021
  Mar. 2021 - Mar. 2021, Japanese, Oral presentation
  共同研究・競争的資金等ID：12898660
• 光合成の強光応答とタンパク質合成系のレドックス制御　　　　　　　　　　　　　　　
  西山佳孝
  Mar. 2021, [Invited]
  Mar. 2021 - Mar. 2021, Japanese, Invited oral presentation
  共同研究・競争的資金等ID：12898660
• 光化学系IIの光阻害と修復の分子機構　　　　　　　　　　　　　　　
  西山佳孝
  Jan. 2021, [Invited]
  Jan. 2021 - Jan. 2021, Japanese, Invited oral presentation
  共同研究・競争的資金等ID：35751334
• 有害赤潮藻 Karenia mikimotoiの遺伝子発現に及ぼす光強度の影響　　　　　　　　　　　　　　　
  紫加田知幸; 西出浩世; 内山郁夫; 高橋文雄; 湯浅光貴; 西山佳孝
  Mar. 2020
• 有害赤潮藻類Chattonella antiquaの活性酸素種産生に及ぼす栄養欠乏の影響　　　　　　　　　　　　　　　
  湯浅光貴; 市川隆祥; 田村悠; 紫加田知幸; 山﨑康裕; 西山佳孝
  Mar. 2020
• 緑藻クラミドモナスにおけるPGRL1の生化学的解析　　　　　　　　　　　　　　　
  高橋拓子; 髙山健太; 井須敦子; 若林憲一; 久堀徹; 西山佳孝
  Mar. 2020
• シロイヌナズナ光合成の強光耐性における葉緑体翻訳因子cpEF-Tuの役割　　　　　　　　　　　　　　　
  新庄梓; 鳥生万智; 西山佳孝
  Mar. 2020
• Synechocystis sp. PCC 6803の超強光順化とカロテノイドによる光化学系IIの光防御機構　　　　　　　　　　　　　　　
  出原太智; 海發育実; 神保晴彦; 高市真一; 西山佳孝
  Mar. 2020
• 有害赤潮形成藻Chattonella marinaのスーパーオキシド産生の生理学的意義　　　　　　　　　　　　　　　
  湯浅光貴; 市川隆祥; 石川優真; 紫加田知幸; 山﨑康裕; 西山佳孝
  Mar. 2020
• 八代海におけるChattonella赤潮の短期動態予測指標　　　　　　　　　　　　　　　
  紫加田知幸; 北辻さほ; 山口聖; 高杉朋孝; 立元伸幸; 湯浅光貴; 西山佳孝
  Jan. 2020
• 懸濁物の炭素・窒素・リン比を用いたChattonella赤潮の動態理解　　　　　　　　　　　　　　　
  山口聖; 紫加田知幸; 北辻さほ; 湯浅光貴; 市川隆祥; 西山佳孝; 立元伸幸; 浦啓介; 高杉朋孝; 向井宏比古; 山口一岩; 多田邦尚
  Dec. 2019
• 赤潮による魚類へい死メカニズム解明へ向けた分子生物学的アプローチ　　　　　　　　　　　　　　　
  紫加田知幸; 北辻さほ; 西槇俊之; 西出浩世; 内山郁夫; 湯浅光貴; 西山佳孝; 尾崎照遵; 秋田一樹; 山﨑康裕
  Dec. 2019
• 光化学系IIの強光順化における翻訳因子EF-Tu の役割　　　　　　　　　　　　　　　
  神保晴彦; 出原太智; 日原由香子; 久堀徹; 西山佳孝
  Nov. 2019, [Domestic conference]
  Japanese, Poster presentation
• 光化学系IIの修復強化による遊離脂肪酸生産株の強光耐性の向上　　　　　　　　　　　　　　　
  髙木健輔; 堀江百香; 高谷信之; 小俣達男; 西山佳孝
  Nov. 2019, [Domestic conference]
  Japanese, Poster presentation
• 光合成の環境応答とタンパク質合成制御　　　　　　　　　　　　　　　
  西山 佳孝
  Nov. 2019, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• 光合成の環境応答とストレス耐性　　　　　　　　　　　　　　　
  西山 佳孝
  Nov. 2019, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• 光合成は修復能力を上げて強光に耐える―光合成の強光耐性の新たな仕組みを解明―　　　　　　　　　　　　　　　
  西山 佳孝
  Oct. 2019, [Domestic conference]
  Japanese, Media report
• 有害赤潮藻Chattonella antiquaにおける活性酸素種産生の制御機構の解析　　　　　　　　　　　　　　　
  市川隆祥; 湯浅光貴; 山﨑康裕; 紫加田知幸; 西山佳孝
  Sep. 2019, [Domestic conference]
  Japanese, Oral presentation
• 有害赤潮藻Chattonella 属における活性酸素種産生の生理学的意義　　　　　　　　　　　　　　　
  湯浅光貴; 市川隆祥; 石川優真; 山﨑康裕; 紫加田知幸; 西山佳孝
  Sep. 2019, [Domestic conference]
  Japanese, Oral presentation
• Strong-light response of photosynthesis and redox regulation of protein synthesis　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Invited Seminar, Kasetsart University, Bangkok, Thailand, Sep. 2019, [Invited], [International conference]
  English, Invited oral presentation
• シロイヌナズナ葉緑体翻訳因子EF-Tuの酸化傷害の分子機構　　　　　　　　　　　　　　　
  鳥生万智; 新庄梓; 西山佳孝
  Sep. 2019, [Domestic conference]
  Japanese, Poster presentation
• Strong-light response of photosynthesis and redox regulation of protein synthesis　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Invited Seminar, King’s Mongkut University of Technology, Thonburi, Bangkok, Thailand, Sep. 2019, [Invited], [International conference]
  English, Invited oral presentation
• 有害赤潮藻類Chattonella属における活性酸素産生と光合成の関係　　　　　　　　　　　　　　　
  湯浅光貴; 紫加田知幸; 山﨑康裕; 西山佳孝
  May 2019, [Domestic conference]
  Japanese, Poster presentation
• 有害赤潮藻類Chattonella antiquaの活性酸素産生と光合成の関係　　　　　　　　　　　　　　　
  湯浅光貴; 鈴木和仁; 紫加田知幸; 北辻さほ; 山﨑康裕; 西山佳孝
  Mar. 2019, [Domestic conference]
  Japanese, Oral presentation
• シアノバクテリアSynechococcus elongatus PCC 7942における翻訳因子EF-Gの酸化傷害の分子機構　　　　　　　　　　　　　　　
  桑野一志; 高木健輔; 是枝晋; 西山佳孝
  Mar. 2019, [Domestic conference]
  Japanese, Poster presentation
• シアノバクテリアSynechocystis sp. PCC 6803の超強光順化におけるカロテノイドの役割　　　　　　　　　　　　　　　
  出原太一; 中澤小夏; 神保晴彦; 高市真一; 西山佳孝
  Mar. 2019, [Domestic conference]
  Japanese, Oral presentation
• Redox regulation of translation and high-light response of photosynthesis　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Institute Seminar, Institute of Tropical Plant Sciences, National Cheng Kung University, Tainan, Taiwan, Nov. 2018, [Invited], [Domestic conference]
  English, Invited oral presentation, National Cheng Kung University, Tainan, Taiwan
• Effects of strong light and high temperature on photosystem II in red tide-forming algae Karenia mikimotoi and Chattonella antiqua　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka; KUWAHARA Yusuke; YUASA Kokia; SHIKATA Tomoyuki
  The 18th International Conference on Harmful Algae, Nantes, France, Oct. 2018, [International conference]
  English, Poster presentation
• Redox regulation of translation and high-light response of photosynthesis　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Institute Seminar, CEA-Grenoble, Grenoble, France, Oct. 2018, [Invited], [Domestic conference]
  English, Invited oral presentation
• Role of translational regulation in the repair of photosystem II　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Japan-Finland Seminar 2018, Kobe, Japan, Sep. 2018, [Invited], [Domestic conference]
  English, Invited oral presentation
• 赤潮藻類Karenia mikimotoiの光合成に及ぼす栄養欠乏と光強度の影響　　　　　　　　　　　　　　　
  湯浅光貴; 紫加田知幸; 西山佳孝
  日本水産学会大会講演要旨集, Sep. 2018
  Japanese
• 有害赤潮藻類Chattonella antiquaの活性酸素発生に及ぼす光と栄養欠乏の影響　　　　　　　　　　　　　　　
  湯浅光貴; 西山佳孝; 紫加田知幸; 北辻さほ; 山崎康裕
  日本ベントス学会・日本プランクトン学会合同大会講演要旨集, Sep. 2018
  Japanese
• シロイヌナズナ葉緑体翻訳因子の酸化傷害と光化学系IIの光阻害　　　　　　　　　　　　　　　
  新庄梓; 鳥生万智; 神保晴彦; 西山佳孝; 西山佳孝
  日本植物学会大会研究発表記録, Sep. 2018
  Japanese
• 中枢代謝を利用した物質生産と光合成能の改変　　　　　　　　　　　　　　　
  小俣達男; 高谷信之; 池田和貴; 愛知真木子; 西山佳孝
  日本生物工学会大会講演要旨集, Aug. 2018
  Japanese
• Role of translational regulation in the repair of photosystem II in Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  16th International Symposium on Photosynthetic Prokaryotes (ISPP2018), The Universty of British Columbeia, Vancouver, Canada, Aug. 2018, [International conference]
  English, Poster presentation
• シアノバクテリアの強光応答におけるサイクリック電子伝達の役割　　　　　　　　　　　　　　　
  高木健輔; 高橋拓子; 西山佳孝
  May 2018, [Domestic conference]
  Japanese, Poster presentation
• 緑藻クラミドモナスのMAPキナーゼによる葉緑体遺伝子psbAの発現制御　　　　　　　　　　　　　　　
  神保晴彦; 西山佳孝; Krishna K. Niyogi
  May 2018, [Domestic conference]
  Japanese, Poster presentation
• 有害赤潮渦鞭毛藻Karenia mikimotoiの生育と光合成に対する強光と貧栄養の影響　　　　　　　　　　　　　　　
  湯浅光貴; 紫加田知幸; 西山佳孝
  May 2018, [Domestic conference]
  Japanese, Poster presentation
• シアノバクテリアSynechocystis sp. PCC 6803 の超強光下における生存戦略　　　　　　　　　　　　　　　
  出原太智; 神保晴彦; 高市真一; 西山佳孝
  Mar. 2018, [Domestic conference]
  Japanese, Poster presentation
• Chlamydomonas reinhardtii の PSI 光防御における PGRL1 の役割　　　　　　　　　　　　　　　
  髙橋拓子; 西山佳孝
  Mar. 2018, [Domestic conference]
  Japanese, Oral presentation
• Synechocystis sp. PCC 6803の強光順化におけるPSII修復能力と翻訳因子EF-Tuの役割　　　　　　　　　　　　　　　
  神保晴彦; 出原太智; 西山佳孝
  Mar. 2018, [Domestic conference]
  Japanese, Oral presentation
• シロイヌナズナの光化学系II光阻害における葉緑体翻訳因子 EF-Tu の役割　　　　　　　　　　　　　　　
  新庄梓; 神保晴彦; 熊木裕香; 西山佳孝
  Mar. 2018, [Domestic conference]
  Japanese, Poster presentation
• 赤潮藻類Karenia mikimotoiの生残,光合成,遊泳に及ぼす貧栄養と強光の影響　　　　　　　　　　　　　　　
  湯浅光貴; 紫加田知幸; 西山佳孝
  日本水産学会大会講演要旨集, Mar. 2018
  Japanese
• Redox regulation of translation and high-light response of photosynthesis　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Department Seminar, University of California, Berkeley, Berkeley, CA, USA, Mar. 2018, [Invited], [Domestic conference]
  English, Invited oral presentation
• Redox regulation of translation and stress response of photosynthesis　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Tokyo Tech CLS International Forum 2018 “Redox regulation of protein function, transcription, translation and folding”, Tokyo, Mar. 2018, [Invited], [Domestic conference]
  English, Invited oral presentation
• Enhanced expression of translation factor EF-Tu accelerates the repair of photosystem II during acclimation to strong light in Synechocystis sp. PCC 6803,　　　　　　　　　　　　　　　
  JIMBO Haruhiko; IZUHARA Taichi; NISHIYAMA Yoshitaka
  Tokyo Tech CLS International Forum 2018 “Redox regulation of protein function, transcription, translation and folding”, Tokyo, Mar. 2018, [Domestic conference]
  English, Poster presentation
• Characterization of PGRL1 in photoprotection of PSI in the green alga Chlamydomonas reinhardtii　　　　　　　　　　　　　　　
  TAKAHASHI Hiroko; NISHIYAMA Yoshitaka
  Tokyo Tech CLS International Forum 2018 “Redox regulation of protein function, transcription, translation and folding”, Tokyo, Mar. 2018, [Domestic conference]
  English, Poster presentation
• 翻訳因子のレドックス制御と光合成の強光応答　　　　　　　　　　　　　　　
  西山 佳孝
  Dec. 2017, [Invited], [Domestic conference]
  Japanese, Oral presentation
• Synechocystis sp. PCC 6803 における光化学系IIの強光順化機構　　　　　　　　　　　　　　　
  神保晴彦; 出原太智; 西山佳孝
  Dec. 2017, [Domestic conference]
  Japanese, Poster presentation
• シアノバクテリア光化学系IIの修復過程におけるオレンジカロテノイドプロテインの役割　　　　　　　　　　　　　　　
  高橋拓子; 李新祥; 山川伯壽; 高市真一; 伊藤繁; 西山佳孝
  Dec. 2017, [Domestic conference]
  Japanese, Poster presentation
• 光合成におけるカロテノイドの機能解析　　　　　　　　　　　　　　　
  西山佳孝
  日本植物学会大会研究発表記録, Sep. 2017
  Japanese
• 緑藻クラミドモナスのPSI光防御におけるPGRL1の役割　　　　　　　　　　　　　　　
  高橋拓子; 曽根和樹; 西山佳孝
  May 2017, [Domestic conference]
  Japanese, Poster presentation
• 翻訳因子EF-Tuの酸化傷害と光化学系IIの修復阻害の関係　　　　　　　　　　　　　　　
  神保晴彦; Rayakorn Yutthanasirikul; 西山佳孝
  May 2017, [Domestic conference]
  Japanese, Poster presentation
• Karenia mikimotoi赤潮衰退時における細胞の鉛直分布,光合成活性および環境条件の日変化　　　　　　　　　　　　　　　
  紫加田知幸; 鬼塚剛; 北辻さほ; 中山奈津子; 松原賢; 阿部和雄; 山口峰生; 湯浅光貴; 桑原悠輔; 西山佳孝; 永井清仁
  日本水産学会大会講演要旨集, Mar. 2017
  Japanese
• Noctiluca scintillansの鉛直分布と有害赤潮藻類に対する摂食　　　　　　　　　　　　　　　
  北辻さほ; 紫加田知幸; 坂本節子; 中山奈津子; 鬼塚剛; 松原賢; 湯浅光貴; 西山佳孝; 多田邦尚
  日本水産学会大会講演要旨集, Mar. 2017
  Japanese
• シアノバクテリア光化学系IIの修復における熱ショックタンパク質DnaK3の役割　　　　　　　　　　　　　　　
  河村大介; 渡辺智; 吉川博文; 西山佳孝
  Mar. 2017, [Domestic conference]
  Japanese, Oral presentation
• シロイヌナズナ葉緑体翻訳因子EF-Tuの酸化傷害の分子機構　　　　　　　　　　　　　　　
  熊木裕香; 小林達巧; 西山佳孝
  Mar. 2017, [Domestic conference]
  Japanese, Poster presentation
• シアノバクテリア光化学系IIの光防御機構におけるオレンジカロテノイドプロテインの役割　　　　　　　　　　　　　　　
  高橋拓子; 草間友里; 李新祥; 高市真一; 伊藤繁; 山川伯壽; 西山佳孝
  Mar. 2017, [Domestic conference]
  Japanese, Oral presentation
• 緑藻クラミドモナスの葉緑体光応答におけるMAPキナーゼの役割　　　　　　　　　　　　　　　
  神保晴彦; Krishna K. Niyogi; 西山佳孝
  Mar. 2017, [Domestic conference]
  Japanese, Oral presentation
• 赤潮渦鞭毛藻Karenia mikimotoiの光合成に対する強光と貧栄養条件の影響　　　　　　　　　　　　　　　
  湯浅光貴; 紫加田知幸; 西山佳孝
  Mar. 2017, [Domestic conference]
  Japanese, Oral presentation
• 光合成の環境応答におけるタンパク質合成系のレドックス制御の役割　　　　　　　　　　　　　　　
  西山 佳孝
  Dec. 2016, [Domestic conference]
  Japanese, Poster presentation
• Effects of temperature stress on photoinhibition of photosystem II in Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Finnish-Japanese Symposium 2016, Saariselkä, Finland, Sep. 2016, [Invited], [Domestic conference]
  English, Invited oral presentation
• Roles of the overexpression of orange carotenoid protein in the protection of photosystem II against photoinhibition in Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  TAKAHASHI Hiroko; KUSAMA Yuri; TAKAICHI Shinichi; ITOH Shigeru; NISHIYAMA Yoshitaka
  Finnish-Japanese Symposium 2016, Saariselkä, Finland, Sep. 2016, [Invited], [Domestic conference]
  English, Oral presentation
• Redox regulation of the repair of photosystem II under photoinhibition　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  The 17th International Photosynthesis Congress, Maastricht, The Netherlands, Aug. 2016, [International conference]
  English, Oral presentation
• 光合成システムの強光応答　　　　　　　　　　　　　　　
  西山 佳孝
  Mar. 2016, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• 赤潮藻類における光化学系IIの強光と高温ストレスに対する応答　　　　　　　　　　　　　　　
  桑原悠輔; 紫加田知幸; 西山佳孝
  Mar. 2016, [Domestic conference]
  Japanese, Oral presentation
• Synergistic effects of iron superoxide dismutase and catalase on the protection of photosynthesis to strong light in Synechococcus elongatus PCC 7942　　　　　　　　　　　　　　　
  SAE-TANG Penporn; 西山佳孝
  Mar. 2016, [Domestic conference]
  English, Oral presentation
• シロイヌナズナ葉緑体翻訳因子EF-GとEF-Tuの酸化ストレス応答　　　　　　　　　　　　　　　
  熊木裕香; 濱川菜桜; 米山拓; 西山佳孝
  Mar. 2016, [Domestic conference]
  Japanese, Poster presentation
• シアノバクテリア光化学系IIの光防御機構におけるオレンジカロテノイドプロテインの機能解析　　　　　　　　　　　　　　　
  髙橋拓子; 草間友里; 李新祥; 西山佳孝
  Mar. 2016, [Domestic conference]
  Japanese, Oral presentation
• 微細藻類における強光阻害現象　　　　　　　　　　　　　　　
  西山 佳孝
  Mar. 2016, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• K.mikimotoiの生理・生態特性　　　　　　　　　　　　　　　
  紫加田知幸; 鬼塚剛; 北辻さほ; 中山奈津子; 湯浅光貴; 西山佳孝; 宮村和良
  瀬戸内海研究フォーラム, 2016
  Japanese
• Regulation and protection of the repair of photosystem II under oxidative stress　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Yamada Conference “International Symposium on Dynamics and Regulation of Photosynthesis”, Nara, Oct. 2015, [Invited], [International conference]
  English, Invited oral presentation
• Photo-oxidative stress to photosynthesis: a new mechanism for photoinhibition of PSII and roles of reactive oxygen species　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Invited Special Seminar, King’s Mongkut University of Technology, Thonburi, Thailand, Sep. 2015, [Invited], [Domestic conference]
  English, Invited oral presentation
• ラフィド藻Chattonella antiquaの単色光に対する走性　　　　　　　　　　　　　　　
  紫加田知幸; 松永茂; 岩堀聖; 桑原悠輔; 西山佳孝
  日本ベントス学会・日本プランクトン学会合同大会講演要旨集, Sep. 2015
  Japanese
• 2014年夏季に宇和島湾で発生したKarenia mikimotoi赤潮 II―衰退に関与した物理化学的要因―　　　　　　　　　　　　　　　
  紫加田知幸; 鬼塚剛; 北辻さほ; 中山奈津子; 阿部和雄; 桑原悠輔; 西山佳孝
  日本水産学会大会講演要旨集, Mar. 2015
  Japanese
• Role of reactive oxygen species in photoinhibition of photosystem II　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  The German-Japanese Binational Seminar 2015, Atami, Mar. 2015, [Invited], [Domestic conference]
  English, Invited oral presentation
• シアノバクテリア光化学系IIの光防御機構における熱放散の役割　　　　　　　　　　　　　　　
  草間友里; 井上修平; 神保晴彦; 園池公毅; 高市真一; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2015
  Japanese
• シアノバクテリアSynechocystis sp.PCC6803における暗条件下での転写因子cyAbrB2の役割　　　　　　　　　　　　　　　
  花井正実; 佐藤雄介; 宮城敦子; 川合真紀; 田中協子; 金子康子; 西山佳孝; 日原由香子
  日本植物生理学会年会要旨集, Mar. 2015
  Japanese
• シアノバクテリア翻訳因子EF‐Tuの酸化傷害機構とその生理学的意義　　　　　　　　　　　　　　　
  神保晴彦; ラヤコーン ユッタナシリクル; 永野孝典; 久堀徹; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2015
  Japanese
• Redox regulation of protein synthesis in photosynthetic organisms　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Tokyo Tech-HHH Dusseldorf Joint Symposium in Photosynthesis as a New Chemical Resource, Tokyo, Mar. 2015, [Invited], [Domestic conference]
  English, Invited oral presentation
• The redox regulation of elongation factor EF-Tu in photoinhibition of photosystem II in Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  JIMBO Haruhiko; YUTTHANASIRIKUL Rayakorn; NAGANO Takanori; NISHIYAMA Yoshitaka
  Tokyo Tech-HHH Dusseldorf Joint Symposium in Photosynthesis as a New Chemical Resource, Tokyo, Mar. 2015, [Domestic conference]
  English, Poster presentation
• Roles of carotenoids in the protection of photosystem II from photoinhibition　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Japan-Finland Binational Seminar 2014, Sapporo, Oct. 2014, [Invited], [Domestic conference]
  English, Invited oral presentation
• 光化学系IIの光阻害に対する高温ストレスの影響　　　　　　　　　　　　　　　
  西山佳孝; 上野護; 草間友里
  日本植物学会大会研究発表記録, Sep. 2014
  Japanese
• Action of reactive oxygen species in photoinhibition of photosystem II　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  Department Seminar, University of California, Berkeley, CA, USA, Mar. 2014, [Invited], [Domestic conference]
  English, Invited oral presentation
• シアノバクテリアの光阻害防御機構における熱放散の役割　　　　　　　　　　　　　　　
  草間友里; 井上修平; 園池公毅; 高市真一; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2014
  Japanese
• 赤潮藻類における光化学系IIの光阻害に対する温度の影響　　　　　　　　　　　　　　　
  桑原悠輔; 濱口卓也; 紫加田知幸; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2014
  Japanese
• シアノバクテリア翻訳因子EF‐Tuの酸化傷害と光化学系IIの強光応答　　　　　　　　　　　　　　　
  神保晴彦; ユッタナシリクル ラヤコーン; 永野孝典; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2014
  Japanese
• 葉緑体翻訳因子EF‐GおよびEF‐Tuの酸化ストレス応答性　　　　　　　　　　　　　　　
  米山拓; 大窪孝幸; 永野孝典; 金森崇; 上田卓也; 久堀徹; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2014
  Japanese
• 赤潮藻Karenia mikimotoiにおける鉛直方向の走性に及ぼす光環境の影響　　　　　　　　　　　　　　　
  紫加田知幸; 坂本節子; 山口峰生; 西山佳孝
  日本水産学会大会講演要旨集, Sep. 2013
  Japanese
• Effects of oxidative damage to the translation factor EF-Tu on photoinhibition of photosystem II in cyanobacterium Synechocystis sp. PCC 6803　　　　　　　　　　　　　　　
  JIMBO Haruhiko; YUTTHANASIRIKUL Rayakorn; NAGANO Takanori; NISHIYAMA Yoshitaka
  16th International Congress on Photosynthesis Research, Saint Louis, USA, Aug. 2013, [International conference]
  English, Poster presentation
• Oxidative damage to protein synthesis during photoinhibition of photosystem II　　　　　　　　　　　　　　　
  NISHIYAMA Yoshitaka
  RSB Seminar, The Australian National University, Canberra, Australia, May 2013, [Invited], [Domestic conference]
  English, Invited oral presentation
• 光化学系IIの光阻害におけるカロテノイドの保護作用　　　　　　　　　　　　　　　
  草間友里; 井上修平; 高市真一; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2013
  Japanese
• 光化学系IIの強光ストレス応答における翻訳因子EF‐Tuの役割　　　　　　　　　　　　　　　
  神保晴彦; YUTTHANASIRIKUL Rayakorn; 永野孝典; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2013
  Japanese
• 大腸菌翻訳系におけるEF‐Gの酸化傷害とレドックス制御の分子機構　　　　　　　　　　　　　　　
  永野孝典; YUTTHANASIRIKUL; Rayakorn; 久堀徹; 金森崇; 竹内(富田)野乃; 上田卓也; 西山佳孝
  日本分子生物学会年会プログラム・要旨集(Web), 2013
  Japanese
• 大腸菌翻訳因子EF‐Gの酸化傷害とレドックス制御の分子機構　　　　　　　　　　　　　　　
  永野孝典; RAYAKORN Yutthanasirikul; 久堀徹; 金森崇; 竹内(富田)野乃; 上田卓也; 西山佳孝
  日本生化学会大会(Web), 2013
  Japanese
• 光合成の光ストレス傷害からの再生機構　　　　　　　　　　　　　　　
  西山佳孝
  旭硝子財団研究助成成果発表会, Jul. 2012
  Japanese
• 穏やかな高温ストレス下における光化学系IIの光阻害の緩和　　　　　　　　　　　　　　　
  上野護; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2012
  Japanese
• タンパク質合成系の改変による光化学系IIの強光耐性の向上　　　　　　　　　　　　　　　
  西山佳孝; 江島加余子
  日本植物生理学会年会要旨集, Mar. 2012
  Japanese
• 通性CAM植物アイスプラント・プラスチド型リン酸輸送体の基質特異性　　　　　　　　　　　　　　　
  是枝晋; 野澤彰; 岡田有右; 隆一輝; 西山佳孝; 大西純一; 戸澤譲
  日本植物生理学会年会要旨集, Mar. 2012
  Japanese
• 光化学系IIの光阻害に対する抗酸化物質の役割　　　　　　　　　　　　　　　
  井上修平; APPEL Jens; 高市真一; 村田紀夫; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2012
  Japanese
• 大腸菌翻訳因子EF‐Gの酸化傷害と翻訳のレドックス制御　　　　　　　　　　　　　　　
  永野孝典; 小島幸治; 久堀徹; 林秀則; 森田勇人; 金森崇; 宮城智子; 上田卓也; 西山佳孝
  日本生化学会大会(Web), 2012
  Japanese
• シアノバクテリア翻訳因子EF‐Gの光合成依存的なレドックス制御　　　　　　　　　　　　　　　
  諸田拓哉; 永野孝典; 小島幸治; 久堀徹; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2011
  Japanese
• 光化学系IIの光阻害におけるα‐トコフェロールの保護作用　　　　　　　　　　　　　　　
  井上修平; 江島加余子; JENS Appel; 林秀則; 村田紀夫; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2011
  Japanese
• Synechocystis sp.PCC6803における光合成電子伝達に依存的な転写因子PedRのチオレドキシンとの相互作用の解析　　　　　　　　　　　　　　　
  門脇太朗; 堀内真由美; 中村絹; 小島幸治; 西山佳孝; 畠山和佳子; 久堀徹; 日原由香子
  日本植物生理学会年会要旨集, Mar. 2011
  Japanese
• シアノバクテリア翻訳系のレドックス制御と環境応答　　　　　　　　　　　　　　　
  西山佳孝
  生化学, 2011
  Japanese
• 大腸菌翻訳因子EF‐Gのレドックス制御機構　　　　　　　　　　　　　　　
  永野孝典; 小島幸治; 林秀則; 金森崇; 宮城智子; 上田卓也; 西山佳孝
  生化学, 2011
  Japanese
• タンパク質合成の強光応答における翻訳因子EF‐Gの役割　　　　　　　　　　　　　　　
  江島加余子; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2010
  Japanese
• シアノバクテリアのSynechocystis sp.PCC6803における光合成電子伝達に依存的な転写因子PedRの解析　　　　　　　　　　　　　　　
  堀内真由美; 中村絹; 小島幸治; 西山佳孝; 畠山和佳子; 久堀徹; 日原由香子
  日本植物生理学会年会要旨集, Mar. 2009
  Japanese
• シアノバクテリアの翻訳因子EF‐Gのレドックス状態を介した翻訳調節　　　　　　　　　　　　　　　
  小島圭治; 諸田拓哉; 日原由香子; 本橋健; 畠山和佳子; 久堀徹; 林秀則; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2009
  Japanese
• ラン藻における翻訳伸長因子EF‐Gの酸化還元と翻訳制御　　　　　　　　　　　　　　　
  小島幸治; 大下将; 久堀徹; 林秀則; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2008
  Japanese
• ラン藻の光化学系IIの高温適応に関与する脂肪酸合成酵素　　　　　　　　　　　　　　　
  南條洋平; 和田元; 林秀則; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2008
  Japanese
• 光化学系IIの光阻害に対するビタミンEの保護作用　　　　　　　　　　　　　　　
  岩井恵理; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2008
  Japanese
• ラン藻の酸化ストレス耐性における翻訳伸長因子EF‐Gの役割　　　　　　　　　　　　　　　
  西山佳孝; 武田祐輔; 井出有紀; 小島幸治; 林秀則
  日本植物生理学会年会要旨集, Mar. 2008
  Japanese
• Synechococcus sp.PCC7002のメタロチオネイン遺伝子のクローニングとその発現様式　　　　　　　　　　　　　　　
  相原加奈子; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2008
  Japanese
• ラン藻の翻訳伸長因子EF‐Gとチオレドキシンとの相互作用　　　　　　　　　　　　　　　
  大下将; 小島幸治; 久堀徹; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2007
  Japanese
• ダイズ培養細胞のチラコイド膜における光化学系IIの高温適応の分子機構　　　　　　　　　　　　　　　
  武智和也; 南條洋平; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2007
  Japanese
• ラン藻のin vitro翻訳系を用いたタンパク質合成系の酸化ストレス傷害の解析　　　　　　　　　　　　　　　
  小島幸治; 大下将; 林秀則; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2007
  Japanese
• 活性酸素消去系酵素を過剰発現させたラン藻における光合成の酸化ストレス耐性　　　　　　　　　　　　　　　
  中野愛; 野田暁子; 奥山英登志; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2007
  Japanese
• タンパク質合成系の酸化ストレス傷害とレドックス制御　　　　　　　　　　　　　　　
  西山佳孝; 小島幸治; 大下将; 久堀徹; 林秀則
  日本植物生理学会年会要旨集, Mar. 2007
  Japanese
• ラン藻の光化学系IIの高温適応に関与するタンパク質の解析　　　　　　　　　　　　　　　
  南條洋平; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2006
  Japanese
• ラン藻Synechocystis sp. PCC6803の無細胞翻訳系の作製とD1タンパク質合成の酸化ストレス感受性　　　　　　　　　　　　　　　
  小島幸治; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2006
  Japanese
• ラン藻のSmtAを改変したポリペプチドによる重金属の蓄積および金属選択性　　　　　　　　　　　　　　　
  中岡美和; 松本亘弘; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2006
  Japanese
• ダイズ培養細胞における光化学系IIの高温傷害と高温適応　　　　　　　　　　　　　　　
  西山佳孝; 南條洋平; 武智和也; 村田紀夫; 林秀則
  日本植物生理学会年会要旨集, Mar. 2006
  Japanese
• ラン藻のSmtAを改変したポリペプチドの金属結合能　　　　　　　　　　　　　　　
  林秀則; 松本亘弘; 中岡美和; 西山佳孝
  日本植物生理学会年会要旨集, Mar. 2005
  Japanese
• ラン藻のADP‐ribose加水分解酵素ファミリーの機能と分子進化　　　　　　　　　　　　　　　
  奥田賢治; 越見由美子; 久高佳奈; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2005
  Japanese
• ラン藻Synechocystis sp. PCC 6803におけるADP‐ribose pyrophosphatase subfamilyの機能解析　　　　　　　　　　　　　　　
  奥田賢治; 西山佳孝; 林秀則
  日本分子生物学会年会プログラム・講演要旨集, Nov. 2004
  Japanese
• クラミドモナスにおける光化学系IIの酸化ストレス傷害の機構　　　　　　　　　　　　　　　
  西山佳孝; 兼松亨; 村田紀夫; 林秀則
  日本植物生理学会年会要旨集, Mar. 2004
  Japanese
• ラン藻におけるADP‐riboseに特異的なNudix hydrolase,NuhAの機能と生理学的役割　　　　　　　　　　　　　　　
  奥田賢治; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2004
  Japanese
• 酵母の重金属輸送P‐type ATPase遺伝子を導入したトランスジェニックシロイヌナズナの重金属耐性　　　　　　　　　　　　　　　
  白石恵美; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2004
  Japanese
• 好冷性細菌の熱ショックタンパク質発現機構の解析　　　　　　　　　　　　　　　
  山内清司; 奥山英登志; 西山佳孝; 林秀則
  日本分子生物学会年会プログラム・講演要旨集, Nov. 2003
  Japanese
• カドミウム耐性に関わるCad2タンパク質の機能解析　　　　　　　　　　　　　　　
  白石恵美; 西山佳孝; 林秀則
  日本分子生物学会年会プログラム・講演要旨集, Nov. 2003
  Japanese
• シアノバクテリアにおけるADP‐riboseに特異的な新規Nudix hydrolase　　　　　　　　　　　　　　　
  奥田賢治; 西山佳孝; 林秀則
  日本分子生物学会年会プログラム・講演要旨集, Nov. 2003
  Japanese
• 光合成と活性酸素　　　　　　　　　　　　　　　
  西山佳孝
  日本化学会西日本大会講演予稿集, Oct. 2003
  Japanese
• 塩ストレスは光化学系IIの光阻害の回復を転写・翻訳過程で阻害する　　　　　　　　　　　　　　　
  ALLAKHVERDIEV S I; 宮入祥夫; 山本宏; 西山佳孝; 兼崎友; 村田紀夫
  日本植物学会大会研究発表記録, Sep. 2002
  Japanese
• 光化学系IIの修復過程における活性酸素の作用機構　　　　　　　　　　　　　　　
  西山佳孝; 山本宏; ALLAKHVERDIEV S I; 村田紀夫
  日本植物生理学会年会要旨集, Mar. 2002
  Japanese
• ラン藻の熱ショック遺伝子のプロモーター領域に結合するタンパク質の機能解析　　　　　　　　　　　　　　　
  奥田賢治; 森田勇人; 佐々木博; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2002
  Japanese
• ラン藻の高温耐性に関与するプラスミドpAQ1の解析　　　　　　　　　　　　　　　
  木村愛子; 森田勇人; 藤博幸; 西山佳孝; 林秀則
  日本植物生理学会年会要旨集, Mar. 2002
  Japanese
• ラン藻の光化学系IIにおける強光と塩ストレスの強調的な阻害作用 NaClによる回復過程の阻害　　　　　　　　　　　　　　　
  ALLAKHVERDIEV S I; 宮入祥夫; 西山佳孝; 村田紀夫
  日本植物学会大会研究発表記録, Sep. 2000
  Japanese
• 光合成の光阻害における活性酸素の作用機構　　　　　　　　　　　　　　　
  西山佳孝; 山本宏; 横田明穂; 村田紀夫
  日本植物生理学会年会要旨集, Mar. 2000
  Japanese
• クラミドモナスのviolaxanthin変換に関与する遺伝子の解明　　　　　　　　　　　　　　　
  加藤彰; ALIA; CHEN T H H; 西山佳孝; 高市真一; 石崎公庸; 福沢秀哉; 村田紀夫
  日本植物生理学会年会要旨集, Mar. 2000
  Japanese
• クラミドモナスの光合成の高温適応 核と葉緑体ゲノムの相互作用　　　　　　　　　　　　　　　
  田中祐二; 西山佳孝; 村田紀夫
  日本植物生理学会年会要旨集, Mar. 2000
  Japanese
• 浸透圧ストレスによるラン藻の光合成の阻害機構 水チャンネルの役割　　　　　　　　　　　　　　　
  西山佳孝; ALLAKHVERDIEV S; 坂本敦; 村田紀夫
  日本植物学会大会研究発表記録, 1999
  Japanese
• ラン藻の光化学系II酸素発生複合体における高温耐性獲得の生理学的意義　　　　　　　　　　　　　　　
  西山佳孝; 村田紀夫
  日本植物生理学会年会要旨集, May 1998
  Japanese
• High temperature resistance of the photosynthetized oxygen generating system in Chlamydomonas adapting to high temperature.　　　　　　　　　　　　　　　
  田中祐二; 西山佳孝; 村田紀夫
  日本植物学会大会研究発表記録, 1997
  Japanese
• Growth of blue-green alga Synechocystis sp. PCC6803 under low temperatures and the role of diene fatty acid of membrane lipid.　　　　　　　　　　　　　　　
  田坂恭嗣; GOMBOS Z; 西山佳孝; 大場哲彦; 大木和夫; 村田紀夫
  日本植物生理学会年会要旨集, Mar. 1996
  Japanese
• 13-kDa protein relating to high temperatura resistance of PCC7002 oxygen evolving complex of blue-green alga Synechococcus sp.　　　　　　　　　　　　　　　
  西山佳孝; LOS D A; 林秀則; 村田紀夫
  日本植物生理学会年会要旨集, Mar. 1996
  Japanese
• Molecular genetics and environmental adaptation of blue-green alga. High temperatura adaptation and high temperatura resistance of blue-green alga.　　　　　　　　　　　　　　　
  林秀則; 西山佳孝; 村田紀夫
  日本遺伝学会大会プログラム・予稿集, Oct. 1995
  Japanese
• ラン藻Synechococcus PCC7002およびダイズ培養細胞における光合成の高温耐性　　　　　　　　　　　　　　　
  西山佳孝; 林秀則; 渡辺正; 村田紀夫
  日本植物生理学会年会要旨集, Mar. 1995
  Japanese
• シアノバクテリアSynechococcus PCC7002の酸素発生の熱安定性におけるシトクロムc‐550の役割　　　　　　　　　　　　　　　
  西山佳孝; 林秀則; 渡辺正; 村田紀夫
  日本植物生理学会年会要旨集, Mar. 1994
  Japanese

• THE BOTANICAL SOCIETY OF JAPAN
• THE JAPANESE SOCIETY OF PHOTOSYNTHESIS RESEARCH
• The Chemical Sciety of Japan
• The Japanese Association for Photosynthesis Research
• The Japanese Association of Plant Physiologists

• Bio-Digital Transformation (バイオDX)産学共創拠点　　　　　　　　　　　　　　　
  2022 - 2031
  Coinvestigator
  Grant amount(Total)：20000000
  Competitive research funding
• Environmental adaptation of photosynthesis in the noxious red-tide-forming raphidophyte Chattonella marina complex　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Transformative Research Areas (A), 01 Apr. 2024 - 31 Mar. 2026
  Saitama University
  Grant amount(Total)：7410000, Direct funding：5700000, Indirect funding：1710000
  Grant number：24H02066
  論文ID：47941760, メディア報道ID：49616964
• Study on the accumulation algorithm of noxious red-tide algae in dioramic and panoramic environments.　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Transformative Research Areas (A), Grant-in-Aid for Transformative Research Areas (A), Sep. 2021 - Mar. 2026
  Fisheries Research and Education Agency, Coinvestigator
  Grant amount(Total)：133510000, Direct funding：102700000, Indirect funding：30810000
  Grant number：21H05305
  論文ID：47941760, 講演・口頭発表等ID：48385250, メディア報道ID：49616964
• 生物メタネーションとバイオ燃料製造を可能とする新排水処理プロセスの開発　　　　　　　　　　　　　　　
  Jul. 2021 - Mar. 2026
  Coinvestigator
  講演・口頭発表等ID：49617742, 産業財産権ID：49617435, メディア報道ID：48384819
• 藻類光合成研究　　　　　　　　　　　　　　　
  Jul. 2024 - Mar. 2025
  Principal investigator
  Grant amount(Total)：2990000, Direct funding：2300000, Indirect funding：690000
  Industry academia cooperation
• 新規FFA生産株の開発　　　　　　　　　　　　　　　
  Jun. 2024 - Mar. 2025
  Principal investigator
  Grant amount(Total)：1583764, Direct funding：1218280, Indirect funding：365483
  Industry academia cooperation
  メディア報道ID：48384819
• 光合成のレドックス制御と環境応答の分子機構　　　　　　　　　　　　　　　
  Apr. 2024 - Mar. 2025
  Principal investigator
  Grant amount(Total)：400000
  Competitive research funding
  論文ID：41702140
• 赤潮被害防止対策技術の開発　　　　　　　　　　　　　　　
  Apr. 2024 - Mar. 2025
  Coinvestigator
  Grant amount(Total)：1300000
• 光化学系II酸素発生系の再生機構　　　　　　　　　　　　　　　
  Apr. 2022 - Mar. 2025
  Grant amount(Total)：4160000, Direct funding：3200000, Indirect funding：960000
  Grant number：22K06259
  論文ID：44092355, 講演・口頭発表等ID：49617705, メディア報道ID：48384831
• 藻類光合成研究　　　　　　　　　　　　　　　
  Jul. 2021 - Mar. 2024
  Coinvestigator
• Study on mechanisms to maintain the function of photosystem I under strong light　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (C), 01 Apr. 2018 - 31 Mar. 2023
  Saitama University
  Grant amount(Total)：4420000, Direct funding：3400000, Indirect funding：1020000
  Grant number：18K06275
  講演・口頭発表等ID：49617692
• 光化学系IIの光阻害と修復の分子機構　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area), Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area), Nov. 2020 - Mar. 2022
  Saitama University, Principal investigator
  Grant amount(Total)：4290000, Direct funding：3300000, Indirect funding：990000
  Grant number：20H05089
  論文ID：41702140, 講演・口頭発表等ID：35770973
• 赤潮被害防止対策技術の開発　　　　　　　　　　　　　　　
  Apr. 2019 - Mar. 2022
  Coinvestigator
  講演・口頭発表等ID：49617831
• ミルキング法によるバイオ燃料生産の高効率化と安定化　　　　　　　　　　　　　　　
  Nov. 2017 - Mar. 2022
  Competitive research funding
  メディア報道ID：31328897
• 光合成の強光耐性におけるタンパク質合成系の順化機構の役割　　　　　　　　　　　　　　　
  Apr. 2018 - Mar. 2021
  Principal investigator
  Competitive research funding
  講演・口頭発表等ID：35770961
• The role of cyclic electron flow in the repair of photosystem II　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Young Scientists (B), Apr. 2016 - Mar. 2019
  Takahashi Hiroko; NISHIYAMA Yoshitaka; TAKAGI Kensuke, Saitama University
  Grant amount(Total)：4290000, Direct funding：3300000, Indirect funding：990000
  Non photochemical quenching (NPQ) is important short-term acclimation in response to high light conditions. Cyanobacteria have Orange Carotenoid Protein (OCP) that quenches excessive light energy as heat. We generated the OCP-deficient and OCP-overexpressed strains. OCP-overexpressed strain showed high NPQ level and tolerance to photoinhibition of photosystem II. Additionally, de novo synthesis of photosystem II protein, D1, was enhanced and also the production of singlet oxygen that inhibits the elongation of translation, was decreased in the overexppressed strain. We concluded that larger extent of NPQ should suppress the production of singlet oxygen via quenching the excitation energy and the elongation process should be protected, resulting in alleviated photo inhibition of photosystem II. This study was published in Plant Cell and Physiology (2019) 60, 367-375.
  Grant number：16K18561
• 光化学系II修復の強光順化メカニズムの解明　　　　　　　　　　　　　　　
  Apr. 2015 - Mar. 2018
  Principal investigator
  Competitive research funding
• タンパク質合成系の改変による光合成の強光ストレス耐性の向上　　　　　　　　　　　　　　　
  Apr. 2013 - Mar. 2015
  Principal investigator
  Competitive research funding, Grant number：25119704
• 光合成における翻訳のレドックス制御と環境応答の分子機構　　　　　　　　　　　　　　　
  Apr. 2012 - Mar. 2015
  Principal investigator
  Competitive research funding
• 光合成の光ストレス傷害からの再生機構　　　　　　　　　　　　　　　
  Apr. 2010 - Mar. 2012
  Principal investigator
  Competitive research funding
• Molecular mechanisms of the redox regulation of translation and the response of photosynthesis to environmental changes　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (C), Apr. 2009 - Mar. 2012
  NISHIYAMA Yoshitaka; HISABORI Toru, Saitama University, Principal investigator
  Elongation factor G, a key protein in translation elongation, was inactivated via the formation of an intramolecular disulfide bond between two specific cysteine residues under oxidative conditions in the cyanobacterium Synechocystissp. PCC 6803. Reduction of the disulfide bond by thioredoxin resulted in the reactivation of EF-G, suggesting that translation might be regulated by the reducing power derived from the photosynthetic electron transport. Replacement of the target cysteine residue of EF-G by serine in Synechocystiscells protected photosystem II from photoinhibition.
  Competitive research funding, Grant number：21570033
• 翻訳のレドックス制御を介する光合成の環境応答の分子機構　　　　　　　　　　　　　　　
  Apr. 2007 - Mar. 2009
  Principal investigator
  Competitive research funding
• Molecular Mechanism of heat-shock response and high-temperature adaptation in psychrophilic bacteria　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (C), 2006 - 2008
  HAYASHI Hidenori; OKUYAMA Hidetoshi; NISHIYAMA Yoshitaka, Ehime University
  Grant amount(Total)：4010000, Direct funding：3500000, Indirect funding：510000
  Grant number：18608003
• Molecular mechanisms of the response of photosynthesis to oxidative stress　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (C), Apr. 2005 - Mar. 2007
  NISHIYAMA Yoshitaka; TOZAWA Yuzuru, Ehime University, Principal investigator
  Ph00otoinhibition of photosystem II (PSII) is due to the imbalance between the rate of photodamage to PSII and the rate of the repair of damaged PSII. Photodamage is initiated by the direct effects of light on the oxygen-evolving complex and, thus, photodamage to PSII is unavoidable. Studies of the effects of oxidative stress on photodamage and subsequent repair have revealed that reactive oxygen species (ROS) act primarily by inhibiting the repair of photodamaged PSII and not by damaging PSII directly. Thus, strong light has dual effects on PSII ; it damages PSII directly and it inhibits the repair of PSII via production of ROS. Investigations of the ROS-induced inhibition of repair have demonstrated that ROS suppress the synthesis de novo of proteins that are required for the repair of PSII, such as the D1 protein. Moreover, analysis of polysomes has determined that a primary target for inhibition by ROS is the elongation step of translation. Investigations using a cyanobacterial translation system in vitro have revealed that elongation factor G might be the primary target, within the translational machinery, of inhibition by ROS. Here we present a new paradigm for the molecular action of ROS in photoinhibition.
  Competitive research funding, Grant number：17570040
• シアノバクテリアの高温適応を制御する遺伝子の網羅的解析　　　　　　　　　　　　　　　
  Apr. 2003 - Mar. 2005
  Principal investigator
  Competitive research funding, Grant number：16013237
• 酸化ストレスによるタンパク質合成系の阻害機構　　　　　　　　　　　　　　　
  Apr. 2002 - Mar. 2004
  Principal investigator
  Competitive research funding, Grant number：14740441
• Studies on low-temperature sensors and the mechanisms of acclimation to low-temperature　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (S), 2001 - 2004
  MURATA Norio; SUZUKI Iwane
  Grant amount(Total)：123370000, Direct funding：94900000, Indirect funding：28470000
  (1) The cyanobacterium Synechocystis sp. PCC 6803 contains 44 genes for histidine kinases (Hiks) and 42 genes for response regulators (Rres). We individually inactivated all of these signal transducers and generated knockout libraries. By screening these libraries by cold-inducible expression of genes with genome-wide DNA microarrays we identified Hik33 as only one Hik for cold sensing and Rre 26 and Rre 31 as response regulators located downstreem of Hik33 in the cold signal transduction pathway.
  (2) We identified Hik33, which we previously identified as a cold sensor, as a component involved in the signal pathways of hyperosmotic, cold, strong-light and oxidative stress. These findings suggest that Hik33 itself is not specific to the individual stress and that the signal transduction pathways which include Hiks and Rres are more complicated than the simple two-component systems which have been established previously. It is very likely that Hik33 cooperates with other factors that give the specificity to individual stress. Identifications of such factors will be an important subject of further study.
  (3) We demonstrated possibilities that some Ser/Thr protein kinases are involved in the cold-signal transduction pathway and that DNA supercoiling may directly sense the cold signals.
  Grant number：13854002
• シアノバクテリアの高温適応を制御する遺伝子群の同定　　　　　　　　　　　　　　　
  2003 - 2003
  Grant amount(Total)：3200000, Direct funding：3200000
  Grant number：15013243
• Molecular mechanism of acclimation and tolerance to low temperature.　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Specially Promoted Research, 1996 - 2000
  MURATA Norio; SUZUKI Iwane; NISHIYAMA Yosyitaka; SAKAMOTO Atsushi, Okazaki National Research Institutes
  Grant amount(Total)：167000000, Direct funding：167000000
  (1) The effect of unsaturated membrane lipids on tolerance to cold and freezing stress : Up to the last year we demonstrated that unsaturated membrane lipids protect the photosynthetic machinery of plants and cyanobacteria against the photoinhibition at low temperature by promoting the repair of photoinhibited photosystem II.In this year, we have elucidated that the unsaturated membrane lipids accelerate the translation of psbA gene for the precursor to D1 protein, and furthermore that they are also important in the tolerance of the photosynthetic machinery to salt stress.
  (2) Protection against cold and freezing stress by glycinebetaine : We previously demonstrated that the genetic manipulation to enable Arabidopsis to synthesize glycinebetaine enhances tolerance to various kinds of environmental stress at various stages of life cycle. In this year we have elucidated that the protective effect of glycinebetaine is based on the promotion of protein synthesis de novo by stabilizing the protein-synthesizing machinery.
  (3) New factors for cold acclimation : The global examination of cold-inducible expression of genes in Synechocystis with DNA microarrays has revealed that cold stress induces a number of genes, which encode factors in transcription and translation, subunit proteins of ribosomes, RNA helicases, and a number of proteins of unknown function. Functions of these proteins in cold acclimation are important subjects of future study.
  (4) Cold sensor and cold signal transduction pathway : Up to the last year, we identified two cold sensors and a cold-signal transducer. In this year, we have applied DNA microarrays to successfully classify cold-inducible genes into three groups according to the regulation of cold inducibility by the cold sensors. Group-1 genes are regulated by the first cold sensor, Group-2 genes are by the second sensor, and Group-3 genes are by both sensors.
  Grant number：08102011

• 遊離脂肪酸生産藻類、および脂肪酸製造方法　　　　　　　　　　　　　　　
  Patent right
  共同研究・競争的資金等ID：35751372
• 遊離脂肪酸生産藻類、および脂肪酸製造方法　　　　　　　　　　　　　　　
  Patent right
  共同研究・競争的資金等ID：35751372
• 遊離脂肪酸の分離方法および遊離脂肪酸生産微生物の培養方法　　　　　　　　　　　　　　　
  Patent right
  共同研究・競争的資金等ID：35751372
• 遊離脂肪酸生産藻類とその製造方法、および脂肪酸製造方法　　　　　　　　　　　　　　　
  Patent right
  共同研究・競争的資金等ID：35751372
• 遊離脂肪酸の製造方法および遊離脂肪酸生産藻類　　　　　　　　　　　　　　　
  Patent right
  共同研究・競争的資金等ID：35751372
• 非遺伝子組換え型の遊離脂肪酸生産藻類とその製造方法、および脂肪酸製造方法　　　　　　　　　　　　　　　
  Patent right
  共同研究・競争的資金等ID：35751372
• 赤潮原因ラフィド藻の光逃避行動を誘導する方法　　　　　　　　　　　　　　　
  Patent right

• Harmful red-tide-forming plankton release reactive oxygen species to maintain photosynthesis capacity — One step toward understanding toxicity to fish　　　　　　　　　　　　　　　
  JST, Science Japan, 21 Nov. 2024, [Internet]
  共同研究・競争的資金等ID：35751341;48384882
• 有害赤潮プランクトン 活性酸素放出で光合成能力維持　　　　　　　　　　　　　　　
  18 Oct. 2024, [Paper]
  共同研究・競争的資金等ID：48384882;35751341
• 有害赤潮プランクトンの活性酸素放出と光合成の関係解明－魚毒性診断技術の確立に向けて－　　　　　　　　　　　　　　　
  26 Sep. 2024, [Others]
  共同研究・競争的資金等ID：48384882;35751341
• 有害赤潮プランクトンの活性酸素放出と光合成の関係解明－魚毒性診断技術の確立に向けて－　　　　　　　　　　　　　　　
  26 Sep. 2024, [Others]
  共同研究・競争的資金等ID：48384882;35751341
• 光合成を“強く”することに成功 －光合成の強光耐性を高める手法を開発－　　　　　　　　　　　　　　　
  21 Nov. 2023, [Others]
  共同研究・競争的資金等ID：43652948;48384882
• 期待の次世代エネルギー!“藻類オイル”最前線　　　　　　　　　　　　　　　
  10 Sep. 2023, [Media report]
  共同研究・競争的資金等ID：35751372;49618086
• 藻類から燃料、CO2実質ゼロ ちとせ研究所が大型施設　　　　　　　　　　　　　　　
  15 Jun. 2023, [Paper]
  共同研究・競争的資金等ID：35751372
• 「油」放出する藻類を開発…大成建設など、バイオ燃料の低コスト化に期待　　　　　　　　　　　　　　　
  24 Apr. 2023, [Paper]
  共同研究・競争的資金等ID：35751372
• 油成分放出の藻類、開発 抽出不要、何度も可能 大成建設など　　　　　　　　　　　　　　　
  19 Apr. 2023, [Paper]
  共同研究・競争的資金等ID：35751372
• 大成建設や埼玉大など、燃料物質である油を細胞外につくる微細藻類を開発 | TECH+（テックプラス）　　　　　　　　　　　　　　　
  18 Apr. 2023, [Internet]
  共同研究・競争的資金等ID：35751372
• 大成建設ら、油を細胞外で生産する藻を作製 バイオ燃料製造コスト減に期待　　　　　　　　　　　　　　　
  17 Apr. 2023, [Internet]
  共同研究・競争的資金等ID：35751372
• 世界初、燃料物質である”油“を細胞外に生産する微細藻類の作製に成功 ―工業利用時の製造や運用に係るコストなどの軽減に期待―　　　　　　　　　　　　　　　
  12 Apr. 2023, [Others]
  共同研究・競争的資金等ID：35751372
• 世界初、燃料物質である“油”を細胞外に生産する微細藻類の作製に成功 | ニュース　　　　　　　　　　　　　　　
  12 Apr. 2023, [Others]
  共同研究・競争的資金等ID：35751372
• 光合成は修復能力を上げて強光に耐える―光合成の強光耐性の新たな仕組みを解明―　　　　　　　　　　　　　　　
  Myself, 01 Oct. 2019, [Others]
  共同研究・競争的資金等ID：12898665