Performance information

• A type II toxin–antitoxin system, ECs3274-ECs3275, in enterohemorrhagic Escherichia coli O157
  Yuka Sasaki; Yuna Mogi; Mizuki Yoshioka; Ke Liu; Yuichi Otsuka
  Bioscience, Biotechnology, and Biochemistry, Volume：89, Number：1, First page：62, Last page：71, Jan. 2025, [Reviewed], [Last, Corresponding]
  Abstract
  
  The toxin–antitoxin (TA) genetic module controls various bacterial events. Novel toxins with different functions are still being discovered. This study aimed to determine whether the ECs3274-ECs3275 gene pair encoded by enterohemorrhagic Escherichia coli O157 functions as a TA system. To characterize this putative TA system, we analyzed the growth of E. coli expressing ECs3274, ECs3275, or both; the interaction between ECs3274 and ECs3275 using bacterial adenylate cyclase two-hybrid assays; and the DNA-binding ability of ECs3274 using gel-mobility shift assays. We observed that the ECs3274 antitoxin interacted with the ECs3275 toxin, was destabilized by Lon protease, and repressed its promoter activity via its helix-turn-helix (HTH) motif. These properties are consistent with those of typical type II TA antitoxins. Interestingly, ECs3275 has an HTH motif not observed in other TA toxins and is necessary for ECs3275 toxicity, suggesting that ECs3275 may exert its toxicity by regulating the expression of specific genes.
  Oxford University Press (OUP), Scientific journal
  DOI：https://doi.org/10.1093/bbb/zbae146
  DOI ID：10.1093/bbb/zbae146, eISSN：1347-6947
• Phage single-stranded DNA-binding protein or host DNA damage triggers the activation of the AbpAB phage defense system.　　　　　　　　　　　　　　　
  Takaomi Sasaki; Saya Takita; Takashi Fujishiro; Yunosuke Shintani; Satoki Nojiri; Ryota Yasui; Tetsuro Yonesaki; Yuichi Otsuka
  mSphere, Volume：8, Number：6, First page：e0037223, Dec. 2023, [Reviewed], [Last, Corresponding], ［International magazine］
  Although numerous phage defense systems have recently been discovered in bacteria, how these systems defend against phage propagation or sense phage infections remains unclear. The Escherichia coli AbpAB defense system targets several lytic and lysogenic phages harboring DNA genomes. A phage-encoded single-stranded DNA-binding protein, Gp32, activates this system similar to other phage defense systems such as Retron-Eco8, Hachiman, ShosTA, Nhi, and Hna. DNA replication inhibitors or defects in DNA repair factors activate the AbpAB system, even without phage infection. This is one of the few examples of activating phage defense systems without phage infection or proteins. The AbpAB defense system may be activated by sensing specific DNA-protein complexes.
  English, Scientific journal
  DOI：https://doi.org/10.1128/msphere.00372-23
  DOI ID：10.1128/msphere.00372-23, PubMed ID：37882551, PubMed Central ID：PMC10732053
• The hokW-sokW Locus Encodes a Type I Toxin–Antitoxin System That Facilitates the Release of Lysogenic Sp5 Phage in Enterohemorrhagic Escherichia coli O157
  Kosuke Takada; Kotone Hama; Takaomi Sasaki; Yuichi Otsuka
  Toxins, Volume：13, Number：11, First page：796, Last page：796, Nov. 2021, [Reviewed], [Last, Corresponding]
  The toxin-antitoxin (TA) genetic modules control various bacterial events, such as plasmid maintenance, persister cell formation, and phage defense. They also exist in mobile genetic elements, including prophages; however, their physiological roles remain poorly understood. Here, we demonstrate that hokW-sokW, a putative TA locus encoded in Sakai prophage 5 (Sp5) in enterohemorrhagic Escherichia coli O157: H7 Sakai strain, functions as a type I TA system. Bacterial growth assays showed that the antitoxic activity of sokW RNA against HokW toxin partially requires an endoribonuclease, RNase III, and an RNA chaperone, Hfq. We also demonstrated that hokW-sokW assists Sp5-mediated lysis of E. coli cells when prophage induction is promoted by the DNA-damaging agent mitomycin C (MMC). We found that MMC treatment diminished sokW RNA and increased both the expression level and inner membrane localization of HokW in a RecA-dependent manner. Remarkably, the number of released Sp5 phages decreased by half in the absence of hokW-sokW. These results suggest that hokW-sokW plays a novel role as a TA system that facilitates the release of Sp5 phage progeny through E. coli lysis.
  MDPI AG, English, Scientific journal
  DOI：https://doi.org/10.3390/toxins13110796
  DOI ID：10.3390/toxins13110796, eISSN：2072-6651, 共同研究・競争的資金等ID：13443555
• Manipulating Interactions between T4 Phage Long Tail Fibers and Escherichia coli Receptors
  Akiyo Suga; Marina Kawaguchi; Tetsuro Yonesaki; Yuichi Otsuka
  Applied and Environmental Microbiology, Volume：87, Number：13, Jul. 2021, [Reviewed], [Last, Corresponding]
  Understanding the host specificity of phages will lead to the development of phage therapy. The interaction between outer membrane protein C (OmpC), one of the Escherichia coli receptors, and the gp37 protein composing the digital tip (DT) region of the long tail fibers of bacteriophage T4 largely determines its host specificity.
  American Society for Microbiology, English, Scientific journal
  DOI：https://doi.org/10.1128/aem.00423-21
  DOI ID：10.1128/aem.00423-21, ISSN：0099-2240, eISSN：1098-5336, 共同研究・競争的資金等ID：13443555;13443556
• A short peptide derived from the ZorO toxin functions as an effective antimicrobial　　　　　　　　　　　　　　　
  Otsuka Y; Ishikawa T; Takahashi C; Masuda M
  Toxins, Volume：11, Number：7, First page：DOI:10.3390/toxins11070392, Jul. 2019, [Reviewed], [Lead, Corresponding], ［International magazine］
  Antimicrobial peptides are potential molecules for the development of novel antibiotic agents. The ZorO toxin of a type I toxin-antitoxin system in Escherichia coli O157:H7 is composed of 29 amino acids and its endogenous expression inhibits E. coli growth. However, little is known about its inhibitory mechanism. In this study, we demonstrate that the ZorO localized in the inner membrane affects the plasma membrane integrity and potential when expressed in E. coli cells, which triggers the production of cytotoxic hydroxyl radicals. We further show that five internal amino acids (Ala-Leu-Leu-Arg-Leu; ALLRL) of ZorO are necessary for its toxicity. This result prompted us to address the potential of the synthetic ALLRL peptide as an antimicrobial. Exogenously-added ALLRL peptide to Gram-positive bacteria, Staphylococcus aureus and Bacillus subtilis, and a fungus, Candida albicans, trigger cell membrane damage and exhibit growth defect, while having no effect on Gram-negative bacterium, E. coli. The ALLRL peptide retains its activity under the physiological salt concentrations, which is in contrast to natural antimicrobial peptides. Importantly, this peptide has no toxicity against mammalian cells. Taken together, an effective and short peptide, ALLRL, would be an attractive antimicrobial to Gram-positive bacteria and C. albicans.
  English, Scientific journal
  DOI：https://doi.org/10.3390/toxins11070392
  DOI ID：10.3390/toxins11070392, PubMed ID：31277504, PubMed Central ID：PMC6669753
• RnlB Antitoxin of the Escherichia coli RnlA-RnlB Toxin-Antitoxin Module Requires RNase HI for Inhibition of RnlA Toxin Activity　　　　　　　　　　　　　　　
  Kenta Naka; Dan Qi; Tetsuro Yonesaki; Yuichi Otsuka
  TOXINS, Volume：9, Number：1, First page：DOI:10.3390/toxins9010029, Jan. 2017, [Reviewed], [Last, Corresponding]
  English, Scientific journal
  DOI：https://doi.org/10.3390/toxins9010029
  DOI ID：10.3390/toxins9010029, ISSN：2072-6651, Web of Science ID：WOS:000392980000029
• Characterization of the interactions between Escherichia coli receptors, LPS and OmpC, and bacteriophage T4 long tail fibers　　　　　　　　　　　　　　　
  Ayaka Washizaki; Tetsuro Yonesaki; Yuichi Otsuka
  MICROBIOLOGYOPEN, Volume：5, Number：6, First page：1003, Last page：1015, Dec. 2016, [Reviewed], [Last, Corresponding]
  English, Scientific journal
  DOI：https://doi.org/10.1002/mbo3.384
  DOI ID：10.1002/mbo3.384, ISSN：2045-8827, Web of Science ID：WOS:000390567300008
• Structural insights into the inhibition mechanism of bacterial toxin LsoA by bacteriophage antitoxin Dmd　　　　　　　　　　　　　　　
  Hua Wan; Yuichi Otsuka; Zeng-Qiang Gao; Yong Wei; Zhen Chen; Michiaki Masuda; Tetsuro Yonesaki; Heng Zhang; Yu-Hui Dong
  MOLECULAR MICROBIOLOGY, Volume：101, Number：5, First page：757, Last page：769, Sep. 2016, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1111/mmi.13420
  DOI ID：10.1111/mmi.13420, ISSN：0950-382X, eISSN：1365-2958, Web of Science ID：WOS:000384410300005
• Prokaryotic toxin-antitoxin systems: novel regulations of the toxins　　　　　　　　　　　　　　　
  Yuichi Otsuka
  CURRENT GENETICS, Volume：62, Number：2, First page：379, Last page：382, May 2016, [Reviewed], [Lead, Corresponding]
  English, Scientific journal
  DOI：https://doi.org/10.1007/s00294-015-0557-z
  DOI ID：10.1007/s00294-015-0557-z, ISSN：0172-8083, eISSN：1432-0983, Web of Science ID：WOS:000373954800022
• An ADP-ribosyltransferase Alt of bacteriophage T4 negatively regulates the Escherichia coli MazF toxin of a toxin-antitoxin module　　　　　　　　　　　　　　　
  Abdulraheem M. Alawneh; Dan Qi; Tetsuro Yonesaki; Yuichi Otsuka
  MOLECULAR MICROBIOLOGY, Volume：99, Number：1, First page：188, Last page：198, Jan. 2016, [Reviewed], [Last, Corresponding]
  English, Scientific journal
  DOI：https://doi.org/10.1111/mmi.13225
  DOI ID：10.1111/mmi.13225, ISSN：0950-382X, eISSN：1365-2958, Web of Science ID：WOS:000369157900013
• Rapid Degradation of Host mRNAs by Stimulation of RNase E Activity by Srd of Bacteriophage T4　　　　　　　　　　　　　　　
  Dan Qi; Abdulraheem M. Alawneh; Tetsuro Yonesaki; Yuichi Otsuka
  GENETICS, Volume：201, Number：3, First page：977, Last page：U356, Nov. 2015, [Reviewed], [Last, Corresponding]
  English, Scientific journal
  DOI：https://doi.org/10.1534/genetics.115.180364
  DOI ID：10.1534/genetics.115.180364, ISSN：0016-6731, eISSN：1943-2631, Web of Science ID：WOS:000365517200014
• AbpA and AbpB provide anti-phage activity in Escherichia coli　　　　　　　　　　　　　　　
  Ryota Yasui; Ayaka Washizaki; Yuko Furihata; Tetsuro Yonesaki; Yuichi Otsuka
  Genes and Genetic Systems, Volume：89, Number：2, First page：51, Last page：60, Sep. 2014, [Reviewed], [Last, Corresponding]
  Genetics Society of Japan, English, Scientific journal
  DOI：https://doi.org/10.1266/ggs.89.51
  DOI ID：10.1266/ggs.89.51, ISSN：1880-5779, PubMed ID：25224971, SCOPUS ID：84907545882
• RNase HI stimulates the activity of RnlA toxin in Escherichia coli　　　　　　　　　　　　　　　
  Kenta Naka; Mitsunori Koga; Tetsuro Yonesaki; Yuichi Otsuka
  MOLECULAR MICROBIOLOGY, Volume：91, Number：3, First page：596, Last page：605, Feb. 2014, [Reviewed], [Last, Corresponding]
  English, Scientific journal
  DOI：https://doi.org/10.1111/mmi.12479
  DOI ID：10.1111/mmi.12479, ISSN：0950-382X, eISSN：1365-2958, Web of Science ID：WOS:000345498000012
• Structure-function studies of Escherichia coli RnlA reveal a novel toxin structure involved in bacteriophage resistance　　　　　　　　　　　　　　　
  Yong Wei; Zeng-Qiang Gao; Yuichi Otsuka; Kenta Naka; Tetsuro Yonesaki; Heng Zhang; Yu-Hui Dong
  MOLECULAR MICROBIOLOGY, Volume：90, Number：5, First page：956, Last page：965, Dec. 2013, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1111/mmi.12409
  DOI ID：10.1111/mmi.12409, ISSN：0950-382X, eISSN：1365-2958, Web of Science ID：WOS:000327374300004
• Identification of the human PMR1 mRNA endonuclease as an alternatively processed product of the gene for peroxidasin-like protein　　　　　　　　　　　　　　　
  Shan-Qing Gu; Baskar Bakthavachalu; Joonhee Han; Deepak P. Patil; Yuichi Otsuka; Chittibabu Guda; Daniel R. Schoenberg
  RNA, Volume：18, Number：6, First page：1186, Last page：1196, Jun. 2012, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1261/rna.031369.111
  DOI ID：10.1261/rna.031369.111, ISSN：1355-8382, eISSN：1469-9001, Web of Science ID：WOS:000304423000008
• Dmd of bacteriophage T4 functions as an antitoxin against Escherichia coli LsoA and RnlA toxins　　　　　　　　　　　　　　　
  Yuichi Otsuka; Tetsuro Yonesaki
  MOLECULAR MICROBIOLOGY, Volume：83, Number：4, First page：669, Last page：681, Feb. 2012, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1111/j.1365-2958.2012.07975.x
  DOI ID：10.1111/j.1365-2958.2012.07975.x, ISSN：0950-382X, Web of Science ID：WOS:000299779200002
• Escherichia coli rnlA and rnlB Compose a Novel Toxin-Antitoxin System　　　　　　　　　　　　　　　
  Mitsunori Koga; Yuichi Otsuka; Sebastien Lemire; Tetsuro Yonesaki
  GENETICS, Volume：187, Number：1, First page：123, Last page：130, Jan. 2011, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1534/genetics.110.121798
  DOI ID：10.1534/genetics.110.121798, ISSN：0016-6731, Web of Science ID：WOS:000286100900010
• IscR Regulates RNase LS Activity by Repressing rnlA Transcription　　　　　　　　　　　　　　　
  Yuichi Otsuka; Kumiko Miki; Mitsunori Koga; Natsu Katayama; Wakako Morimoto; Yasuhiro Takahashi; Tetsuro Yonesaki
  GENETICS, Volume：185, Number：3, First page：823, Last page：830, Jul. 2010, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1534/genetics.110.114462
  DOI ID：10.1534/genetics.110.114462, ISSN：0016-6731, Web of Science ID：WOS:000281906800010
• 新世代のファージ研究　　　　　　　　　　　　　　　
  米崎哲朗; 大塚裕一
  Volume：62, First page：55, Last page：58, 2010, [Last]
  Japanese, Research institution
• Identification of a Cytoplasmic Complex That Adds a Cap onto 5 '-Monophosphate RNA　　　　　　　　　　　　　　　
  Yuichi Otsuka; Nancy L. Kedersha; Daniel R. Schoenberg
  MOLECULAR AND CELLULAR BIOLOGY, Volume：29, Number：8, First page：2155, Last page：2167, Apr. 2009, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1128/MCB.01325-08
  DOI ID：10.1128/MCB.01325-08, ISSN：0270-7306, Web of Science ID：WOS:000264558400015
• APPROACHES FOR STUDYING PMR1 ENDONUCLEASE-MEDIATED MRNA DECAY　　　　　　　　　　　　　　　
  Yuichi Otsuka; Daniel R. Schoenberg
  RNA TURNOVER IN EUKARYOTES: NUCLEASES, PATHWAYS AND ANAYLSIS OF MRNA DECAY, Volume：448, First page：241, Last page：263, 2008, [Reviewed], [Lead]
  English, In book
  DOI：https://doi.org/10.1016/S0076-6879(08)02613-X
  DOI ID：10.1016/S0076-6879(08)02613-X, ISSN：0076-6879, Web of Science ID：WOS:000262252300013
• A role of Rn1A in the RNase LS activity from Escherichia coli　　　　　　　　　　　　　　　
  Yuichi Otsuka; Mitsunori Koga; Akira Iwamoto; Tetsuro Yonesaki
  GENES & GENETIC SYSTEMS, Volume：82, Number：4, First page：291, Last page：299, Aug. 2007, [Reviewed], [Lead]
  English, Scientific journal
  ISSN：1341-7568, eISSN：1880-5779, Web of Science ID：WOS:000250609000003
• Polysome-bound endonuclease PMR1 is targeted to stress granules via stress-specific binding to TIA-1　　　　　　　　　　　　　　　
  Feng Yang; Yong Peng; Elizabeth L. Murray; Yuichi Otsuka; Nancy Kedersha; Daniel R. Schoenberg
  MOLECULAR AND CELLULAR BIOLOGY, Volume：26, Number：23, First page：8803, Last page：8813, Dec. 2006, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1128/MCB.00090-06
  DOI ID：10.1128/MCB.00090-06, ISSN：0270-7306, Web of Science ID：WOS:000242203700012
• A novel endoribonuclease, RNase LS, in Escherichia coli.　　　　　　　　　　　　　　　
  Otsuka Y; Yonesaki T
  Genetics, Volume：169, First page：13, Last page：20, Jan. 2005, [Reviewed], [Lead]
  English, Scientific journal
  CiNii Articles ID：10024394672
• A Novel Endoribonuclease of Escherichia coli that Induces Gene Silencing in Bacteriophage T4　　　　　　　　　　　　　　　
  Yuichi Otsuka
  Osaka University, Dec. 2003, [Lead, Corresponding]
  English, Doctoral thesis
• 大腸菌mRNAの分解　　　　　　　　　　　　　　　
  大塚裕一; 米崎哲朗
  Volume：48, Number：3, First page：240, Last page：246, Mar. 2003, [Reviewed], [Lead]
  Japanese, Others
  ISSN：0039-9450, CiNii Articles ID：40005690889, CiNii Books ID：AN00140437
• Escherichia coli endoribonucleases involved in cleavage of bacteriophage T4 mRNAs　　　　　　　　　　　　　　　
  Y Otsuka; H Ueno; T Yonesaki
  JOURNAL OF BACTERIOLOGY, Volume：185, Number：3, First page：983, Last page：990, Feb. 2003, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1128/JB.185.3.983-990.2003
  DOI ID：10.1128/JB.185.3.983-990.2003, ISSN：0021-9193, Web of Science ID：WOS:000180834300031
• Gene 61.3 of bacteriophage t4 is the spackle gene　　　　　　　　　　　　　　　
  T Kai; H Ueno; Y Otsuka; W Morimoto; T Yonesaki
  VIROLOGY, Volume：260, Number：2, First page：254, Last page：259, Aug. 1999, [Reviewed]
  English, Scientific journal
  ISSN：0042-6822, Web of Science ID：WOS:000082027100005

• RNA Damage and Repair　　　　　　　　　　　　　　　
  Yuichi Otsuka, [Joint work], Endoribonucleases of the toxin-antitoxin systems induce abortive infection
  Kotta-Loizou Ioly・Springer, Jul. 2021
  ISBN：9783030765712, 共同研究・競争的資金等ID：36529828;13443556

• 細菌とファージの生存競争　　　　　　　　　　　　　　　
  大塚裕一
  Mar. 2023, [Invited]
  Invited oral presentation
• The arms race between bacteria and phages ~toxin–antitoxin systems~　　　　　　　　　　　　　　　
  Yuichi Otsuka
  Nov. 2018, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• この世はウイルスだらけ　　　　　　　　　　　　　　　
  大塚裕一
  Dec. 2017, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• 細菌とファージの生存戦略：トキシン－アンチトキシン系の制御　　　　　　　　　　　　　　　
  大塚裕一
  Dec. 2016, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• 細菌のトキシン－アンチトキシン系とファージ感染との関係　　　　　　　　　　　　　　　
  大塚裕一
  Mar. 2016, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• ファージ療法・T4ファージを用いた新しいチャレンジ　　　　　　　　　　　　　　　
  大塚裕一
  Sep. 2014, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• Toxin–Antitoxin Systems in Escherichia coli O157 and Bacteriophage T4 Infection　　　　　　　　　　　　　　　
  Yuichi Otsuka
  Jul. 2012, [Invited], [International conference]
  English, Oral presentation
• トキシン－アンチトキシンとT4ファージ　　　　　　　　　　　　　　　
  大塚裕一
  Sep. 2010, [Invited], [Domestic conference]
  Japanese, Invited oral presentation
• 5' capping of endonuclease-generated decay intermediates by a cytoplasmic capping enzyme complex　　　　　　　　　　　　　　　
  Yuichi Otsuka
  Keystone Symposia 2008: Translational Regulatory Mechanisms, Jan. 2010, [Invited], [International conference]
  English, Invited oral presentation

• Present
• Present
• Present
• Present, JAPANESE SOCIETY FOR BACTERIOLOGY
• Present, THE MOLECULAR BIOLOGY SOCIETY OF JAPAN

• A novel antiphage mechanism suppresses the spread of drug-resistant bacteria　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (C), 01 Apr. 2023 - 31 Mar. 2026
  Saitama University
  Grant amount(Total)：4810000, Direct funding：3700000, Indirect funding：1110000
  Grant number：23K06526
• The toxin–antitoxin systems suppress the expansion of antimicrobial resistant bacteria　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C), Grant-in-Aid for Scientific Research (C), Apr. 2020 - Mar. 2024
  Saitama University, Principal investigator
  Grant amount(Total)：4290000, Direct funding：3300000, Indirect funding：990000
  Grant number：20K07493
  書籍等出版物ID：36829728
• Repression of the spread of antimicrobial resistant bacteria and pathogenic bacteria using the bacterial toxin-antitoxin system　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C), Grant-in-Aid for Scientific Research (C), Apr. 2017 - Mar. 2021
  Otsuka Yuichi, Principal investigator
  Grant amount(Total)：4810000, Direct funding：3700000, Indirect funding：1110000
  The toxin-antitoxin (TA) system is a genetic module composed of a toxin and its cognate antitoxin. The ZorO toxin in Escherichia coli O157 is composed of 29 amino acids and its endogenous expression inhibits E. coli growth. Here, we demonstrated that the ZorO localized in the inner membrane affects the plasma membrane integrity. We further showed that five internal amino acids (Ala-Leu-Leu-Arg-Leu; ALLRL) of ZorO are necessary for its toxicity. Exogenously-added ALLRL peptide to Gram-positive bacteria, S. aureus and B. subtilis, and a fungus, C. albicans, trigger cell membrane damage and exhibit growth defect. Importantly, this peptide has no toxicity against mammalian cells. Taken together, an effective and short peptide, ALLRL, would be an attractive antimicrobial to Gram-positive bacteria and C. albicans. Furthermore, we demonstrated that the TA system suppresses the transduction which is one of the mechanisms that lead to the horizontal gene transfer.
  Grant number：17K08837
  論文ID：36529263
• The functional analysis and the application of bacterial toxin-antitoxin system　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Young Scientists (B), Grant-in-Aid for Young Scientists (B), Apr. 2013 - Mar. 2017
  Otsuka Yuichi; TADA Shunsuke; TAKAHASHI Chisato, Principal investigator
  Grant amount(Total)：4420000, Direct funding：3400000, Indirect funding：1020000
  Toxin-antitoxin system (TAS) is widely conserved in prokaryotic plasmids and chromosomes and is linked to many roles in cell physiology. TAS is composed of a stable toxin that inhibits one of essential cellular processes, and a labile antitoxin that inhibits a harmful effect of the cognate toxin. In this study, the new TAS, z3289-sRNA1, encoded by the Enterohemorrhagic E. coli O157:H7 chromosome has been characterized. I elucidated the molecular mechanism of the toxicity caused by the z3289 toxin, the mechanism for the translational repression of the z3289 toxin by the sRNA1 antitoxin, and the physiological role of z3289-sRNA1 as an anti-phage defense. In addition, I demonstrated that the modified z3289 toxin functions as an antimicrobial peptide.
  Grant number：25870386
  論文ID：36529314, 書籍等出版物ID：36829728
• Inspection of mechanism for recognition of host by phage　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C), Grant-in-Aid for Scientific Research (C), Apr. 2011 - Mar. 2015
  YONESAKI Tetsuro; OTSUKA Yuichi, Osaka University, Coinvestigator
  Grant amount(Total)：5200000, Direct funding：4000000, Indirect funding：1200000
  T4 adsorption to E. coli K12 strain depends on the presence of OmpC, but T4 can adsorb to B strain independently of OmpC. Using K12 mutants defective in various genes required for LPS synthesis, we systematically analyzed the adsorption of T4 phage to these mutants dependent on or independent of OmpC. Furthermore, we isolated T4 mutants which can adsorb to B strain but not to K12 strain or vice versa. These results strongly suggest that T4 has two different mechanisms for adsorption to host cells. In addition, present study identified specific structures in OmpC and the distal tip of T4 long tail fiber, required for the recognition of OmpC by T4.
  Grant number：23570211
• Relationship of cytoplasmic capping to translation and cell stress　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Research Activity Start-up, Grant-in-Aid for Research Activity Start-up, Apr. 2009 - Mar. 2011
  OTSUKA Yuichi, Osaka University, Principal investigator
  Grant amount(Total)：2574000, Direct funding：1980000, Indirect funding：594000
  The purpose of this research project is to verify that capping can occur in cytoplasm as well as nucleus, and show the significance of cytoplasmic capping in gene expression. I identified many target mRNAs to which cap structures would be added in cytoplasm. Also, deep sequencing analysis suggested that some of these mRNAs might have poly(U) tail at 3' terminus. These modifications on mRNA may play important roles in gene expression. In a different research project, I showed that bacteriophage T4 had an antitoxin against E.coli toxins for its own survival.
  Grant number：21870020
• Relationship of cytoplasmic capping to translation and cell stress　　　　　　　　　　　　　　　
  American Heart Association, Grants-in-Aid for Scientific Research, Grant-in-Aid for Research Activity Start-up, Jul. 2008 - Mar. 2009
  Yuichi Otsuka, Osaka University, Principal investigator
  The purpose of this research project is to verify that capping can occur in cytoplasm as well as nucleus, and show the significance of cytoplasmic capping in gene expression. I identified many target mRNAs to which cap structures would be added in cytoplasm. Also, deep sequencing analysis suggested that some of these mRNAs might have poly(U) tail at 3' terminus. These modifications on mRNA may play important roles in gene expression. In a different research project, I showed that bacteriophage T4 had an antitoxin against E.coli toxins for its own survival.
  Competitive research funding, Grant number：21870020
• Relationship of cytoplasmic capping to translation and mRNA decay　　　　　　　　　　　　　　　
  American Heart Association, Jul. 2006 - Jun. 2008
  Yuichi Otsuka, Principal investigator
  Competitive research funding

• サイエンスらいおんカフェ Vol.63 微生物カフェ 〜ウイルスと細菌の終わりなき戦い〜　　　　　　　　　　　　　　　
  lecturer
  03 Mar. 2018
• 栃木県立宇都宮女子高等学校SSH　　　　　　　　　　　　　　　
  lecturer, advisor
  Apr. 2017 - Mar. 2018
• 栃木県高等学校教育研究会理科部会 科学研究会　　　　　　　　　　　　　　　
  lecturer
  15 Nov. 2017
• 高校生のためのウイルス学体験講座　　　　　　　　　　　　　　　
  lecturer
  Aug. 2014 - Aug. 2017