Updated on 2025/06/23

写真b

 
SHIOMI Daisuke
 
*Items subject to periodic update by Rikkyo University (The rest are reprinted from information registered on researchmap.)
Affiliation*
College of Science Department of Life Science
Graduate School of Science Doctoral Program in Life Science
Graduate School of Science Master's Program in Life Science
Title*
Professor
Degree
博士（理学） （ 名古屋大学大学院理学研究科 ）
Research Interests

  • L-form

  • タンパク質間相互作用

  • 細胞形態

  • 形態

  • Bacterial two-hybrid

  • 細胞極性

  • 好熱菌

  • 極性

  • 細胞長

  • 細胞幅

  • 再構成系

  • ペプチドグリカン

  • 大腸菌

  • 形態形成

  • 蛍光タンパク質

  • 抑圧変異体

  • 免疫染色

  • 微生物

  • 細胞膜

  • 細胞骨格タンパク質

  • 低温感受性

  • 細胞分裂

  • 次世代ゲノムシークエンス

  • 細胞骨格

  • 細胞生物学

    • Campus Career*
    • 4 2020 - Present 
      College of Science   Department of Life Science   Professor
    • 4 2020 - Present 
      Graduate School of Science   Master's Program in Life Science   Professor
    • 4 2020 - Present 
      Graduate School of Science   Doctoral Program in Life Science   Professor
    • 4 2013 - 3 2020 
      College of Science   Department of Life Science   Associate Professor
    • 4 2013 - 3 2020 
      Graduate School of Science   Master's Program in Life Science   Associate Professor
    • 4 2013 - 3 2020 
      Graduate School of Science   Doctoral Program in Life Science   Associate Professor

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    Research Areas

    • Life Science / Applied microbiology

    • Life Science / Bacteriology

    • Life Science / Cell biology

    • Life Science / Molecular biology

    Research History

    • 4 2020 - Present 
      立教大学   理学部生命理学科   教授

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    • 4 2013 - Present 
      Rikkyo University   Department of Life Science, College of Science

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    • 1 2008 - 3 2013 
      National Institute of Genetics

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    • 4 2004 - 12 2007 
      University of Texas Houston

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    • 10 2002 - 3 2004 
      Nagoya University   School of Science

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    • 4 2002 - 9 2002 
      名古屋大学大学院   理学研究科   生命理学専攻 DC2

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    Education

    • 4 2000 - 9 2002 
      名古屋大学大学院   理学研究科   生命理学専攻 博士課程 後期

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    • 4 1998 - 3 2000 
      名古屋大学大学院   理学研究科   生命理学専攻 博士課程 前期

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    • 4 1994 - 3 1998 
      Nagoya University   School of Science

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    Committee Memberships

    • 1 2024 - Present 
      日本ゲノム微生物学会   評議員

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      Committee type：Academic society

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    • 1 2018 - 12 2020 
      日本ゲノム微生物学会   会計監査

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      Committee type：Academic society

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    • 1 2018 - 12 2020 
      日本細菌学会   シンポジウム企画調整委員

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      Committee type：Academic society

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    • 1 2015 - 12 2017 
      日本細菌学会   広報委員

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      Committee type：Academic society

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    Awards

    • 6 2025  
      第21回21世紀大腸菌研究会  ポスター発表優秀賞  必須遺伝子の発現抑制と大腸菌 L-form における必須性の検証
       
      尾澤 菜月 (M1)

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    • 6 2023  
      第19回21世紀大腸菌研究会  口頭発表賞  大腸菌の桿菌-L-form 変換時におけるゲノム DNA の動態解析
       
      遠山 唯(M1)

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    • 6 2022  
      第18回21世紀大腸菌研究会  口頭部門発表賞 
       
      山口 穂野香 (M2)

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    • 8 2021  
      第17回21世紀大腸菌研究会  優秀発表賞（ポスター発表部門） 
       
      浪川結衣 (B4)

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    • 3 2021  
      第15回日本ゲノム微生物学会年会  ポスター賞（優秀賞） 
       
      林匡史 (PD)

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    • 3 2021  
      第15回日本ゲノム微生物学会年会  ポスター賞（優秀賞） 
       
      山口穂野香 (B4)

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    • 10 2020  
      第103回日本細菌学会関東支部会  最優秀学生発表賞 
       
      近田大基 (M2)

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    • 8 2019  
      第13回細菌学若手コロッセウム  優秀発表賞 
       
      阿合理沙 (M2)

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    • 5 2019  
      第16回21世紀大腸菌研究会優秀口頭発表賞 
       
      近田大基 (M1)

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    • 11 2018  
      第101回 日本細菌学会関東支部総会  学生優秀発表賞 
       
      阿合理沙 (M1)

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    • 5 2018  
      第15回 21世紀大腸菌研究会  優秀口頭発表賞 
       
      阿合理沙 (M1)

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    • 3 2014  
      日本細菌学会  黒屋奨学賞  細菌形態形成制御機構に関する研究
       
      塩見 大輔

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    Papers

    • Spiroplasma eriocheiris FtsZ assembles the ring-like structure assisted by SepF. Peer-reviewed International journal

      Taishi Kasai, Yuhei O Tahara, Makoto Miyata, Daisuke Shiomi

      The Journal of biological chemistry   108373 - 108373   3 3 2025

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      The FtsZ protein is involved in bacterial cell division. In cell-walled bacteria, such as Bacillus subtilis, FtsZ forms a ring-like structure, called the Z ring, at the cell division site and acts as a scaffold for cell wall synthesis. The inhibition of cell wall synthesis in B. subtilis has been shown to interfere with the function of the Z ring, causing a loss in cell division control. Spiroplasma, a cell wall-less bacterium, lacks most of the genes involved in cell division; however, the ftsZ gene remains conserved. The function of Spiroplasma eriocheiris FtsZ (SeFtsZ) remains to be determined. In the present study, we analyzed the biochemical characteristics of SeFtsZ. Purified SeFtsZ demonstrated lower polymerization capacity and GTPase activity than FtsZ from Escherichia coli and B. subtilis. We also investigated the relationship between SeFtsZ and SeSepF, which anchors FtsZ to the cell membrane, and found that SeSepF did not contribute to the stability of FtsZ filaments, unlike the B. subtilis SepF. SeFtsZ and SeSepF were produced in E. coli L-forms, where cell wall synthesis was inhibited. SeFtsZ formed ring-like structures in cell wall-less E. coli cells, suggesting that SeFtsZ forms Z rings and is involved in cell division independently of cell wall synthesis.

      DOI： 10.1016/j.jbc.2025.108373

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    • Septal wall synthesis is sufficient to change ameba-like cells into uniform oval-shaped cells in Escherichia coli L-forms. Peer-reviewed International journal

      Masafumi Hayashi, Chigusa Takaoka, Koichi Higashi, Ken Kurokawa, William Margolin, Taku Oshima, Daisuke Shiomi

      Communications biology7 ( 1 ) 1569   26 11 2024

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      A cell wall is required to control cell shape and size to maintain growth and division. However, some bacterial species maintain their morphology and size without a cell wall, calling into question the importance of the cell wall to maintain shape and size. It has been very difficult to examine the dispensability of cell wall synthesis in rod-shaped bacteria such as Escherichia coli for maintenance of their shape and size because they lyse without cell walls under normal culture conditions. Here, we show that wall-less E. coli L-form cells, which have a heterogeneous cell morphology, can be converted to a mostly uniform oval shape solely by FtsZ-dependent division, even in the absence of cylindrical cell wall synthesis. This FtsZ-dependent control of cell shape and size in the absence of a cell wall requires at least either the Min or nucleoid occlusion systems for positioning FtsZ at mid cell division sites.

      DOI： 10.1038/s42003-024-07279-y

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    • 細菌の新奇生存戦略:L-form 細胞壁が有っても無くても細菌は生きられる

      塩見大輔, 林匡史, 大島拓

      化学と生物62 ( 1 )   1 1 2024

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      Authorship：Lead author   Language：Japanese  

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    • Relationship between the Rod complex and peptidoglycan structure in Escherichia coli Peer-reviewed

      Risa Ago, Yuhei O. Tahara, Honoka Yamaguchi, Motoya Saito, Wakana Ito, Kaito Yamasaki, Taishi Kasai, Sho Okamoto, Taiki Chikada, Taku Oshima, Issey Osaka, Makoto Miyata, Hironori Niki, Daisuke Shiomi

      MicrobiologyOpen12 ( 5 )   9 10 2023

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1002/mbo3.1385

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    • D-amino Acids Ameliorate Experimental Colitis and Cholangitis by Inhibiting Growth of Proteobacteria: Potential Therapeutic Role in Inflammatory Bowel Disease. Peer-reviewed International journal

      Satoko Umeda, Tomohisa Sujino, Kentaro Miyamoto, Yusuke Yoshimatsu, Yosuke Harada, Keita Nishiyama, Yoshimasa Aoto, Keika Adachi, Naoki Hayashi, Kimiko Amafuji, Nobuko Moritoki, Shinsuke Shibata, Nobuo Sasaki, Masashi Mita, Shun Tanemoto, Keiko Ono, Yohei Mikami, Jumpei Sasabe, Kaoru Takabayashi, Naoki Hosoe, Toshihiko Suzuki, Toshiro Sato, Koji Atarashi, Toshiaki Teratani, Haruhiko Ogata, Nobuhiro Nakamoto, Daisuke Shiomi, Hiroshi Ashida, Takanori Kanai

      Cellular and molecular gastroenterology and hepatology   9 8 2023

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      Language：English   Publishing type：Research paper (scientific journal)  

      BACKGROUND & AIMS: D-amino acids, the chiral counterparts of protein L-amino acids, were primarily produced and utilized by microbes, including those in the human gut. However, little was known about how orally administered or microbe-derived D-amino acids affected the gut microbial community or gut disease progression. METHODS: The ratio of D- to L-amino acids was analysed in feces and blood from patients with ulcerative colitis (UC) and healthy controls. Also, composition of microbe was analysed from patients with UC. Mice treated with D- amino acid in DSS colitis model and liver cholangitis model. RESULTS: The ratio of D- to L-amino acids was lower in the feces of patients with UC than that of healthy controls. Supplementation of D-amino acids ameliorated UC-related experimental colitis and liver cholangitis by inhibiting growth of Proteobacteria. Addition of D-alanine, a major building block for bacterial cell wall formation, to culture medium inhibited expression of the ftsZ gene required for cell fission in the Proteobacteria Escherichia coli and Klebsiella pneumoniae, thereby inhibiting growth. Overexpression of ftsZ restored growth of E. coli even when D-alanine was present. We found that D-alanine not only inhibited invasion of pathological K. pneumoniae into the host via pore formation in intestinal epithelial cells but also inhibited growth of E. coli and generation of antibiotic-resistant strains. CONCLUSION: D-aa might have potential for use in novel therapeutic approaches targeting Proteobacteria-associated dysbiosis and antibiotic-resistant bacterial diseases by means of their effects on the intestinal microbiota community.

      DOI： 10.1016/j.jcmgh.2023.08.002

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    • Outer Membrane is Critical for Viability of Cell Wall-deficient Bacterial Cells, L-form Invited Peer-reviewed

      Daisuke SHIOMI, Taku OSHIMA

      Seibutsu Butsuri63 ( 1 ) 27 - 29   1 2023

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      Authorship：Lead author,　Corresponding author   Publishing type：Research paper (scientific journal)   Publisher：Biophysical Society of Japan  

      DOI： 10.2142/biophys.63.27

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    • 壁をなくしてみたところ Invited Peer-reviewed

      大島 拓, 塩見 大輔

      生物工学会誌100 ( 3 ) 137 - 137   3 2022

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      DOI： 10.34565/seibutsukogaku.100.3_1

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    • Direct Observation of Conversion From Walled Cells to Wall-Deficient L-Form and Vice Versa in Escherichia coli Indicates the Essentiality of the Outer Membrane for Proliferation of L-Form Cells. Peer-reviewed International journal

      Taiki Chikada, Tomomi Kanai, Masafumi Hayashi, Taishi Kasai, Taku Oshima, Daisuke Shiomi

      Frontiers in microbiology12   645965 - 645965   3 2021

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      Gram-negative bacteria such as Escherichia coli are surrounded by an outer membrane, which encloses a peptidoglycan layer. Even if thinner than in many Gram-positive bacteria, the peptidoglycan in E. coli allows cells to withstand turgor pressure in hypotonic medium. In hypertonic medium, E. coli treated with a cell wall synthesis inhibitor such as penicillin G form wall-deficient cells. These so-called L-form cells grow well under anaerobic conditions (i.e., in the absence of oxidative stress), becoming deformed and dividing as L-form. Upon removal of the inhibitor, they return to the walled rod-shaped state. Recently, the outer membrane was reported to provide rigidity to Gram-negative bacteria and to strengthen wall-deficient cells. However, it remains unclear why L-form cells need the outer membrane for growth. Using a microfluidic system, we found that, upon treatment with the outer membrane-disrupting drugs polymyxin B and polymyxin B nonapeptide or with the outer membrane synthesis inhibitor CHIR-090, the cells lysed during cell deformation and division, indicating that the outer membrane was important even in hypertonic medium. L-form cells could return to rod-shaped when trapped in a narrow space, but not in a wide space, likely due to insufficient physical force. Outer membrane rigidity could be compromised by lack of outer membrane proteins; Lpp, OmpA, or Pal. Deletion of lpp caused cells to lyse during cell deformation and cell division. In contrast, ompA and pal mutants could be deformed and return to small oval cells even when less physical force was exerted. These results strongly suggest that wall-deficient E. coli cells require a rigid outer membrane to survive, but not too rigid to prevent them from changing cell shape.

      DOI： 10.3389/fmicb.2021.645965

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    • Alteration of Membrane Fluidity or Phospholipid Composition Perturbs Rotation of MreB Complexes in Escherichia coli. Peer-reviewed International journal

      Keisuke Kurita, Fumiya Kato, Daisuke Shiomi

      Frontiers in molecular biosciences7   582660 - 582660   2020

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      Gram-negative bacteria such as Escherichia coli are surrounded by inner and outer membranes and peptidoglycan in between, protecting the cells from turgor pressure and maintaining cell shape. The Rod complex, which synthesizes peptidoglycan, is composed of various proteins such as a cytoplasmic protein MreB, a transmembrane protein RodZ, and a transpeptidase PBP2. The Rod complex is a highly motile complex that rotates around the long axis of a cell. Previously, we had reported that anionic phospholipids (aPLs; phosphatidylglycerol and cardiolipin) play a role in the localization of MreB. In this study, we identified that cells lacking aPLs slow down Rod complex movement. We also found that at higher temperatures, the speed of movement increased in cells lacking aPLs, suggesting that membrane fluidity is important for movement. Consistent with this idea, Rod complex motion was reduced, and complex formation was disturbed in the cells depleted of FabA or FabB, which are essential for unsaturated fatty acid synthesis. These cells also showed abnormal morphology. Therefore, membrane fluidity is important for maintaining cell shape through the regulation of Rod complex formation and motility.

      DOI： 10.3389/fmolb.2020.582660

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    • RodZ: A key-player in cell elongation and cell division in Escherichia coli Invited Peer-reviewed International journal

      Risa Ago, Daisuke Shiomi

      AIMS Microbiology5 ( 4 ) 358 - 367   11 2019

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.3934/microbiol.2019.4.358

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    • Division-site localization of RodZ is required for efficient Z ring formation in Escherichia coli. Peer-reviewed International journal

      Yoshii Y, Niki H, Shiomi D

      Molecular microbiology111 ( 5 ) 1229 - 1244   5 2019

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      Bacteria such as Escherichia coli must coordinate cell elongation and cell division. Elongation is regulated by an elongasome complex containing MreB actin and the transmembrane protein RodZ, which regulates assembly of MreB, whereas division is regulated by a divisome complex containing FtsZ tubulin. These complexes were previously thought to function separately. However, MreB has been shown to directly interact with FtsZ to switch to cell division from cell elongation, indicating that these complexes collaborate to regulate both processes. Here, we investigated the role of RodZ in the regulation of cell division. RodZ localized to the division site in an FtsZ-dependent manner. We also found that division-site localization of MreB was dependent on RodZ. Formation of a Z ring was delayed by deletion of rodZ, suggesting that division-site localization of RodZ facilitated the formation or stabilization of the Z ring during early cell division. Thus, RodZ functions to regulate MreB assembly during cell elongation and facilitates the formation of the Z ring during cell division in E. coli.

      DOI： 10.1111/mmi.14217

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    • Relation between rotation of MreB actin and cell width of Escherichia coli. Peer-reviewed International journal

      Kurita K, Shin R, Tabei T, Shiomi D

      Genes to cells : devoted to molecular & cellular mechanisms24 ( 3 ) 259 - 265   3 2019

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      Bacterial cells, including Escherichia coli and Bacillus subtilis, continuously elongate and divide. Although the cell width is maintained during cell cycle, the molecular mechanisms involved in its regulation remain unknown. MreB has been implicated to play a role in maintaining cell width. Several point mutations in mreB that affect cell width have been identified. The MreB protein forms clusters or polymers in the cell and moves along annular tracks perpendicular to the long axis. This rotation is coupled with peptidoglycan synthesis. Here, we focused on two MreB mutants, MreBA125V and MreBA174T . Cells producing MreBA125V and MreBA174T were thinner and thicker than WT cells, and MreBA125V and MreBA174T rotated faster and slower than WT MreB, respectively. We observed that the rotation rate correlated with the cell wall synthesis rate. Thus, we conclude that the velocity of MreB rotation also affects cell width, that is, the faster the MreB rotates, the thinner the cell width is.

      DOI： 10.1111/gtc.12667

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    • Regulations of Subcellular Localization and Functions of MreB Actin in Escherichia coli

      栗田恵輔, 塩見大輔

      生物物理(Web)59 ( 2 ) 100‐102(J‐STAGE)   2019

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    • The periplasmic disordered domain of RodZ promotes its self-interaction in Escherichia coli Peer-reviewed International journal

      Ryosuke Ikebe, Yuri Kuwabara, Taiki Chikada, Hironori Niki, Daisuke Shiomi

      Genes to Cells23 ( 4 ) 307 - 317   1 4 2018

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Blackwell Publishing Ltd  

      DOI： 10.1111/gtc.12572

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    • Erratum: Author Correction: ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli (Scientific reports (2017) 7 1 (3492))

      Hiroki Irieda, Daisuke Shiomi

      Scientific reports8 ( 1 ) 4876   15 3 2018

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      Language：English   Publishing type：Research paper (scientific journal)   Publisher：NLM (Medline)  

      DOI： 10.1038/s41598-018-23160-5

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    • Bacterial heterologous expression system for reconstitution of chloroplast inner division ring and evaluation of its contributors Peer-reviewed International journal

      Hiroki Irieda, Daisuke Shiomi

      International Journal of Molecular Sciences19 ( 2 )   11 2 2018

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      Language：English   Publishing type：Research paper (scientific journal)   Publisher：MDPI AG  

      DOI： 10.3390/ijms19020544

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    • Polar localization of MreB actin is inhibited by anionic phospholipids in the rod-shaped bacterium Escherichia coli (vol 63, pg 849, 2017) Invited Peer-reviewed

      Daisuke Shiomi

      CURRENT GENETICS63 ( 5 ) 845 - 848   10 2017

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      Authorship：Corresponding author   Language：English  

      DOI： 10.1007/s00294-017-0701-z

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    • ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli Peer-reviewed

      Hiroki Irieda, Daisuke Shiomi

      SCIENTIFIC REPORTS7 ( 1 ) 3492   6 2017

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1038/s41598-017-03698-6

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    • Exclusion of assembled MreB by anionic phospholipids at cell poles confers cell polarity for bidirectional growth Peer-reviewed

      Takuma Kawazura, Kanon Matsumoto, Koki Kojima, Fumiya Kato, Tomomi Kanai, Hironori Niki, Daisuke Shiomi

      MOLECULAR MICROBIOLOGY104 ( 3 ) 472 - 486   5 2017

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      Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1111/mmi.13639

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    • Rapid, precise quantification of bacterial cellular dimensions across a genomic-scale knockout library Peer-reviewed

      Tristan Ursell, Timothy K. Lee, Daisuke Shiomi, Handuo Shi, Carolina Tropini, Russell D. Monds, Alexandre Colavin, Gabriel Billings, Ilina Bhaya-Grossman, Michael Broxton, Bevan Emma Huang, Hironori Niki, Kerwyn Casey Huang

      BMC BIOLOGY15 ( 1 ) 17   2 2017

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      Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1186/s12915-017-0348-8

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    • Regulation of bacterial cell shape revealed by single cell observations Invited

      Daisuke Shiomi

      Microscopy65   i9 - i9   2016

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      Language：English   Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press  

      DOI： 10.1093/jmicro/dfw044

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    • [Regulation of determination of bacterial shape]. Peer-reviewed

      Shiomi D

      Nihon saikingaku zasshi. Japanese journal of bacteriology69 ( 4 ) 557 - 564   2014

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      Language：Japanese   Publishing type：Research paper (scientific journal)  

      DOI： 10.3412/jsb.69.557

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    • A mutation in the promoter region of zipA, a component of the divisome, suppresses the shape defect of RodZ-deficient cells Peer-reviewed

      Daisuke Shiomi, Hironori Niki

      MICROBIOLOGYOPEN2 ( 5 ) 798 - 810   10 2013

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      Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1002/mbo3.116

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    • Mutations in cell elongation genes mreB, mrdA and mrdB suppress the shape defect of RodZ-deficient cells Peer-reviewed

      Daisuke Shiomi, Atsushi Toyoda, Tomoyuki Aizu, Fumio Ejima, Asao Fujiyama, Tadasu Shini, Yuji Kohara, Hironori Niki

      MOLECULAR MICROBIOLOGY87 ( 5 ) 1029 - 1044   3 2013

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      Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1111/mmi.12148

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    • A mutation of ispA that is involved in isoprenoid biogenesis can improve growth of Escherichia coli at low temperatures Peer-reviewed

      Daisuke Shiomi, Hironori Niki

      MICROBIOLOGY AND IMMUNOLOGY55 ( 12 ) 885 - 888   12 2011

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      Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1111/j.1348-0421.2011.00391.x

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    • Visualization of bacteriophage P1 infection by cryo-electron tomography of tiny Escherichia coli Peer-reviewed

      Jun Liu, Cheng-Yen Chen, Daisuke Shiomi, Hironori Niki, William Margolin

      VIROLOGY417 ( 2 ) 304 - 311   9 2011

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      Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1016/j.virol.2011.06.005

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    • Identification of Escherichia coli ZapC (YcbW) as a Component of the Division Apparatus That Binds and Bundles FtsZ Polymers Peer-reviewed

      Cynthia A. Hale, Daisuke Shiomi, Bing Liu, Thomas G. Bernhardt, William Margolin, Hironori Niki, Piet A. J. de Boer

      JOURNAL OF BACTERIOLOGY193 ( 6 ) 1393 - 1404   3 2011

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      Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1128/JB.01245-10

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    • Mechanism of rod-shape formation by cytoskeletal proteins in Escherichia coli

      SHIOMI Daisuke, NIKI Hironori

      Biseibutsu seitai24 ( 2 ) 51 - 60   1 9 2009

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      Language：Japanese   Publisher：日本微生物生態学会  

      DOI： 10.20709/jsmeja.24.2_51

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    • Genetic mechanism regulating bacterial cell shape and metabolism

      Daisuke Shiomi, Hideo Mori, Hironori Niki

      Communicative and Integrative Biology2 ( 3 ) 219 - 220   5 2009

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      Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.4161/cib.2.3.7930

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    • Determination of bacterial rod shape by a novel cytoskeletal membrane protein Peer-reviewed

      Daisuke Shiomi, Masako Sakai, Hironori Niki

      EMBO JOURNAL27 ( 23 ) 3081 - 3091   12 2008

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      Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1038/emboj.2008.234

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    • Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function Peer-reviewed

      Daisuke Shiomi, William Margolin

      MOLECULAR MICROBIOLOGY67 ( 3 ) 558 - 569   2 2008

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      DOI： 10.1111/j.1365-2958.2007.06085.x

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    • 大腸菌におけるタンパク質の細胞内局在とそのメカニズム

      塩見大輔

      生化学80 ( 1 ) 36 - 40   25 1 2008

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    • Mechanisms Underlying Subcellular Localization of the Bacterial Transmembrane Chemoreceptor

      SHIOMI Daisuke, KAWAGISHI Ikuro

      Biophysics48 ( 1 ) 30 - 34   25 1 2008

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      Language：Japanese   Publisher：日本生物物理学会  

      The chemoreceptors of Escherichia coli cluster at a cell pole, a property which is critical for signaling. However, little is known about the mechanism of polar localization. Our recent study demonstrated that the aspartate chemoreceptor (Tar)-GFP fusion protein is inserted into lateral membrane regions and migrates to the pole. Unexpectedly, Tar-GFP was found to be arranged into a coil, which reflects a coil of the Sec protein translocation machinery. The Sec coil appeared distinct from the coil of MreB, an actin-like cytoskeletal protein. These findings shed new light on the spatial organ...

      DOI： 10.2142/biophys.48.030

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    • [Mechanism underlying subcellular localization of proteins in Escherichia coli]. Peer-reviewed

      Shiomi D

      Seikagaku. The Journal of Japanese Biochemical Society80   36 - 40   1 2008

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    • Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring Peer-reviewed

      Daisuke Shiomi, William Margolin

      MOLECULAR MICROBIOLOGY66 ( 6 ) 1396 - 1415   12 2007

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      DOI： 10.1111/j.1365-2958.2007.05998.x

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    • A sweet sensor for size-conscious bacteria Peer-reviewed

      Daisuke Shiomi, William Margolin

      CELL130 ( 2 ) 216 - 218   7 2007

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    • An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli Peer-reviewed

      Christophe S. Bernard, Mahalakshmi Sadasivam, Daisuke Shiomi, William Margolin

      MOLECULAR MICROBIOLOGY64 ( 5 ) 1289 - 1305   6 2007

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      DOI： 10.1111/j.1365-2958.2007.05738.x

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    • The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring Peer-reviewed

      Brett Geissler, Daisuke Shiomi, William Margolin

      MICROBIOLOGY-SGM153 ( 3 ) 814 - 825   3 2007

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      DOI： 10.1099/mic.0.2006/001834-0

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    • The C-terminal domain of MinC inhibits assembly of the Z ring in Escherichia coli Peer-reviewed

      Daisuke Shiomi, William Margolin

      JOURNAL OF BACTERIOLOGY189 ( 1 ) 236 - 243   1 2007

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      Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1128/JB.00666-06

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    • Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery Peer-reviewed

      D Shiomi, M Yoshimoto, M Homma, Kawagishi, I

      MOLECULAR MICROBIOLOGY60 ( 4 ) 894 - 906   5 2006

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      DOI： 10.1111/j.1365-2958.2006.05145.x

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    • Stabilization of polar localization of a chemoreceptor via its covalent modifications and its communication with a different chemoreceptor Peer-reviewed

      D Shiomi, S Banno, M Homma, Kawagishi, I

      JOURNAL OF BACTERIOLOGY187 ( 22 ) 7647 - 7654   11 2005

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      DOI： 10.1128/JB.187.22.7647-7654.2005

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    • Targeting of the chemotaxis methylesterase/deamidase CheB to the polar receptor-kinase cluster in an Escherichia coli cell Peer-reviewed

      S Banno, D Shiomi, M Homma, Kawagishi, I

      MOLECULAR MICROBIOLOGY53 ( 4 ) 1051 - 1063   8 2004

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      DOI： 10.1111/j.1365-2958.2004.04176.x

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    • Simultaneous measurement of sensor-protein dynamics and motility of a single cell by on-chip microcultivation system. Peer-reviewed International journal

      Ippei Inoue, Daisuke Shiomi, Ikuro Kawagishi, Kenji Yasuda

      Journal of nanobiotechnology2 ( 1 ) 4 - 4   30 4 2004

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      Language：English   Publisher：1  

      Measurement of the correlation between sensor-protein expression, motility and environmental change is important for understanding the adaptation process of cells during their change of generation. We have developed a novel assay exploiting the on-chip cultivation system, which enabled us to observe the change of the localization of expressed sensor-protein and the motility for generations. Localization of the aspartate sensitive sensor protein at two poles in Escherichia coli decreased quickly after the aspartate was added into the cultivation medium. However, it took more than three generations for recovering the localization after the removal of aspartate from the medium. Moreover, the tumbling frequency was strongly related to the localization of the sensor protein in a cell. The results indicate that the change of the spatial localization of sensor protein, which was inherited for more than three generations, may contribute to cells, motility as the inheritable information.

      DOI： 10.1186/1477-3155-2-4

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    • Attractant binding alters arrangement of chemoreceptor dimers within its cluster at a cell pole Peer-reviewed

      M Homma, D Shiomi, M Homma, Kawagishi, I

      PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA101 ( 10 ) 3462 - 3467   3 2004

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      DOI： 10.1073/pnas.0306660101

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    • Dual recognition of the bacterial chemoreceptor by chemotaxis-specific domains of the CheR methyltransferase Peer-reviewed

      D Shiomi, IB Zhulin, M Homma, Kawagishi, I

      JOURNAL OF BIOLOGICAL CHEMISTRY277 ( 44 ) 42325 - 42333   11 2002

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      DOI： 10.1074/jbc.M202001200

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    • Intragenic suppressors of a mutation in the aspartate chemoreceptor gene that abolishes binding of the receptor to methyltransferase Peer-reviewed

      D Shiomi, M Homma, Kawagishi, I

      MICROBIOLOGY-SGM148   3265 - 3275   10 2002

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    • The aspartate chemoreceptor Tar is effectively methylated by binding to the methyltransferase mainly through hydrophobic interaction Peer-reviewed

      D Shiomi, H Okumura, M Homma, Kawagishi, I

      MOLECULAR MICROBIOLOGY36 ( 1 ) 132 - 140   4 2000

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      Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

      DOI： 10.1046/j.1365-2958.2000.01834.x

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    Misc.

    • Mutational analysis of the methyltransferase-binding sequence of the bacterial chemoreceptor, which is critical for chemotactic adaptation

      SHIOMI Daisuke, OKUMURA Hisashi, HOMMA Michio, KAWAGISHI Ikuro

      The Japanese journal of taste and smell research5 ( 3 ) 527 - 528   1 12 1998

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    • Mutational analysis of the carboxy-terminal sequence of the chemoreceptor that serves as the binding site for methyltransferase CheR

      Shiomi D., Okumura H., Homma M., Kawagishi I.

      Biophysics38 ( 2 ) S185   7 9 1998

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      Language：Japanese   Publisher：The Biophysical Society of Japan General Incorporated Association  

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    Presentations

    • 大腸菌 L-form の増殖に関わる機能未知タンパク質 YobH の機能の解明

      西川 芽衣亜, 鳥居 晃, 田原 悠平, 小山田 莉子, 宮田 真人, 大島 拓, 塩見 大輔

      第21回21世紀大腸菌研究会  12 6 2025 

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      Event date： 12 6 2025 - 13 6 2025

      Language：Japanese  

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    • 大腸菌の mlaC 遺伝子欠損による外膜小胞放出と L-form の関連性

      難波 千夢, 大島 拓, 塩見 大輔

      第21回21世紀大腸菌研究会  12 6 2025 

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      Event date： 12 6 2025 - 13 6 2025

      Language：Japanese   Presentation type：Poster presentation  

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    • 大腸菌 L-form における RapA の欠損がもたらす影響

      小松 泰士, 角田 恵太郎, 大島 拓, 塩見 大輔

      第21回21世紀大腸菌研究会  12 6 2025 

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      Event date： 12 6 2025 - 13 6 2025

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    • 必須遺伝子の発現抑制と大腸菌 L-form における必須性の検証

      尾澤 菜月, 杉本 竜太, 石田 一紗, 大塚 香乃, 大島 拓, 塩見 大輔

      第21回21世紀大腸菌研究会  12 6 2025 

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      Event date： 12 6 2025 - 13 6 2025

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    • ミニマルセルを用いた細胞分裂装置形成に必要な最小因子の研究 Invited

      清水大輝, 吉永芳佳, 林匡史, 塩見大輔

      第52回日本マイコプラズマ学会学術集会  24 5 2025 

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      Event date： 23 5 2025 - 24 5 2025

      Language：Japanese   Presentation type：Oral presentation (invited, special)  

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    • ペニシリンによる細胞壁代謝異常は呼吸の亢進を介して細胞壁を必要としない大腸菌L-formの生育を妨げる

      斉藤 元弥, 伊藤 わかな, 近田 大基, 塩見 大輔, 大島 拓

      第19回日本ゲノム微生物学会年会  17 3 2025 

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      Event date： 17 3 2025 - 19 3 2025

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    • 古くて新しいバクテリアの薬剤耐性状態L-formについて Invited

      塩見大輔

      宮崎大学医学部セミナー  27 2 2025 

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      Language：Japanese   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

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    • 最小ゲノムを持つ細菌を用いたFtsZの局在解析

      清水大輝, 林匡史, 佐藤彩翔, 塩見大輔

      第107回日本細菌学会関東支部総会  14 12 2024 

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      Event date： 14 12 2024

      Language：Japanese   Presentation type：Oral presentation (general)  

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    • Biochemical Analysis of Cell Division Protein FtsZ of Haloplasma contractile

      8 8 2024 

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      Event date： 7 8 2024 - 9 8 2024

      Language：Japanese   Presentation type：Poster presentation  

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    • Analysis of subcellular localization of FtsZ in bacteria with the minimum genome

      7 8 2024 

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      Event date： 7 8 2024 - 9 8 2024

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    • Reconstitution of Haloplasma contractile cell wall in JCVI-syn3.0

      7 8 2024 

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      Event date： 7 8 2024 - 9 8 2024

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    • 大腸菌の L-form への変換及び桿菌復帰時におけるゲノム DNA の動態

      遠山唯, 浪川結衣, 大島拓, 塩見大輔

      第20回21世紀大腸菌研究会  17 6 2024 

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      Event date： 17 6 2024 - 18 6 2024

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    • Septal cell wall synthesis is sufficient to change amoeba-like morphology to oval cell shape in Escherichia coli L-form cells.

      Masafumi Hayashi, Chigusa Takaoka, Koichi Higashi, Ken Kurokawa, William Margolin, Taku Oshima, Daisuke Shiomi

      EMBO workshop "Archaeal and bacterial cell division, Beyond the Z-ring"  15 5 2024 

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      Event date： 14 5 2024 - 17 5 2024

      Language：English   Presentation type：Poster presentation  

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    • バクテリアの増殖にとって細胞壁は必要？不必要？ Invited

      塩見大輔

      大隅財団 微生物コンソーシアム定例会  4 4 2024 

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      Event date： 4 4 2024 - 4 4 2024

      Language：Japanese   Presentation type：Oral presentation (invited, special)  

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    • 人工細菌を用いたハロプラズマ細胞壁の再構築

      笠井大司, 田原悠平, 水谷雅希, 柿澤茂行, 宮田真人, 加藤真悟, 塩見大輔

      2023年度国立遺伝学研究所研究会「微生物の細胞複製システムから紐解く生命のデザイン」  29 3 2024 

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      Event date： 28 3 2024 - 29 3 2024

      Language：Japanese   Presentation type：Oral presentation (general)  

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    • バクテリアの未知の生存形態：L-form Invited

      塩見大輔

      生物の基礎探究会  18 3 2024 

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      Event date： 18 3 2024 - 19 3 2024

      Language：Japanese   Presentation type：Oral presentation (general)  

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    • ハロプラズマのDCWクラスターを中心とした細胞壁合成遺伝子の解析

      笠井大司, 加藤真悟, 塩見大輔

      第18回日本ゲノム微生物学会年会  12 3 2024 

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      Event date： 12 3 2024 - 14 3 2024

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    • 大腸菌の桿菌-L-form 変換時におけるゲノム DNA の動態解析

      遠山唯, 浪川結衣, 大島拓, 塩見大輔

      第19回21世紀大腸菌研究会  30 6 2023 

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      Event date： 29 6 2023 - 30 6 2023

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    • 機能未知遺伝子yobHのL-form増殖への影響

      鳥居晃, 小山田莉子, 大島拓, 塩見大輔

      第19回21世紀大腸菌研究会  29 6 2023 

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      Event date： 29 6 2023 - 30 6 2023

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    • 大腸菌を用いた二重膜細胞から一重膜細胞への進化の過程の再現

      阿蒜侑佳, 近田大基, 大島拓, 塩見大輔

      第19回21世紀大腸菌研究会  29 6 2023 

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      Event date： 29 6 2023 - 30 6 2023

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    • 細胞分裂の位置決定メカニズムが細胞の形を制御する

      林匡史, 高岡ちぐさ, 東光一, 黒川顕, 大島拓, 塩見大輔

      第19回21世紀大腸菌研究会  29 6 2023 

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      Event date： 29 6 2023 - 30 6 2023

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    • 細胞壁を持たない細菌の細胞分裂タンパク質[DS1] を用いたL型大腸菌の分裂制御

      笠井大司, 田原悠平, 宮田真人, 塩見大輔

      第19回21世紀大腸菌研究会  29 6 2023 

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      Event date： 29 6 2023 - 30 6 2023

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    • 大腸菌細胞壁修復に関わるSanAタンパク質の解析

      山口穂野香, 阿合理沙, 田原悠平, 笠井大司, 宮田真人, 塩見大輔

      2022年度国立遺伝学研究所研究会  30 3 2023 

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      Event date： 30 3 2023 - 31 3 2023

      Language：Japanese   Presentation type：Oral presentation (general)  

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    • 細胞壁のない細菌の細胞分裂タンパク質の相互作用解析

      笠井 大司, 田原 悠平, 宮田 真人, 塩見 大輔

      第96回日本細菌学会総会  17 3 2023 

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      Event date： 16 3 2023 - 18 3 2023

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    • FtsZ 依存的な細胞分裂による細胞サイズ制御

      林 匡史, 高岡 ちぐさ, 大島 拓, 塩見 大輔

      第17回日本ゲノム微生物学会年会  10 3 2023 

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      Event date： 8 3 2023 - 10 3 2023

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    • 大腸菌ペプチドグリカン修復関連因子の複合体構造予測と相互作用解析

      山口 穂野香, 阿合 理沙, 田原 悠平, 笠井 大司, 宮田 真人, 塩見 大輔

      第17回日本ゲノム微生物学会年会  8 3 2023 

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      Event date： 8 3 2023 - 10 3 2023

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    • 細胞壁を持たない大腸菌L-formにおけるゲノムDNAの動態解析

      遠山 唯, 浪川 結衣, 大島 拓, 塩見 大輔

      第17回日本ゲノム微生物学会年会  8 3 2023 

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      Event date： 8 3 2023 - 10 3 2023

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    • スパイロプラズマのFtsZタンパク質が構築する構造のL型大腸菌を用いた解析

      笠井 大司, 田原 悠平, 宮田 真人, 塩見 大輔

      第17回日本ゲノム微生物学会年会  8 3 2023 

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      Event date： 8 3 2023 - 10 3 2023

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    • バクテリアの生存戦略：バクテリアは細胞壁無しでどのように生存できるのか？ Invited

      塩見大輔

      大分大学グローカル感染症研究センター セミナー  16 12 2022 

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    • 細胞壁に覆われていない大腸菌が見せる特異な表情 Invited

      塩見 大輔

      第45回日本分子生物学会年会  2 12 2022 

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      Event date： 30 11 2022 - 2 12 2022

      Language：Japanese   Presentation type：Oral presentation (invited, special)  

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    • Functional analysis of Spiroplasma cell division proteins

      30 9 2022 

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      Event date： 28 9 2022 - 30 9 2022

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    • 大腸菌L-formの増殖過程と桿菌への復帰過程におけるZ-ringの制御メカニズム

      林 匡史, 高岡 ちぐさ, 大島 拓, 塩見 大輔

      第16回細菌学若手コロッセウム  25 8 2022 

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      Event date： 25 8 2022 - 27 8 2022

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    • 大腸菌L-formからの復帰過程における外膜と細胞壁のリンクの役割

      阿蒜 侑佳, 近田 大基, 大島 拓, 塩見 大輔

      第18回21世紀大腸菌研究会  28 6 2022 

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      Event date： 27 6 2022 - 28 6 2022

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    • スパイロプラズマFtsZとSepFの相互作用とGTPase活性

      笠井大司, 田原悠平, 宮田真人, 塩見大輔

      第18回21世紀大腸菌研究会  28 6 2022 

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      Event date： 27 6 2022 - 28 6 2022

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    • SanAが関与する大腸菌のペプチドグリカン修復機構の解析

      山口穂野香, 阿合理沙, 田原悠平, 笠井大司, 宮田真人, 塩見大輔

      第18回21世紀大腸菌研究会  27 6 2022 

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      Event date： 27 6 2022 - 28 6 2022

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    • ペプチドグリカン合成の活性化とZ-ring収縮開始メカニズムの関係性

      林匡史, 高岡ちぐさ, 大島拓, 塩見大輔

      第18回21世紀大腸菌研究会  27 6 2022 

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      Event date： 27 6 2022 - 28 6 2022

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    • Direct observation of proliferation of cell wall-deficient Escherichia coli cells

      塩見 大輔, 林 匡史, 浪川 結衣, 高岡 ちぐさ, 大島 拓

      第95回日本細菌学会総会（オンライン）  29 3 2022 

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      Event date： 29 3 2022 - 31 3 2022

      Presentation type：Symposium, workshop panel (nominated)  

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    • バクテリアの柔軟な細胞増殖形態の変化 Invited

      塩見 大輔, 林 匡史, 近田 大基, 浪川 結衣, 高岡 ちぐさ, 大島 拓

      日本農芸化学会 2022年度 京都大会（オンライン）  16 3 2022 

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      Event date： 15 3 2022 - 18 3 2022

      Presentation type：Oral presentation (invited, special)  

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    • 大腸菌の特殊な増殖様式

      塩見 大輔

      2021年度国立遺伝学研究所研究会「単細胞システムの複製と維持における生体高分子の機能」  9 3 2022 

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      Event date： 8 3 2022 - 9 3 2022

      Presentation type：Oral presentation (general)  

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    • 細胞壁合成の制御による、Z-ring 収縮開始メカニズムの探索

      林 匡史, 高岡 ちぐさ, 大島 拓, 塩見 大輔

      第16回日本ゲノム微生物学会年会（オンライン）ポスター発表  4 3 2022 

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      Event date： 2 3 2022 - 4 3 2022

      Presentation type：Oral presentation (general)  

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    • 抗生物質の違いによる大腸菌L-formの代謝変化

      伊藤 わかな, 塩見 大輔, 大島 拓

      第16回日本ゲノム微生物学会年会（オンライン）  3 3 2022 

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      Event date： 2 3 2022 - 4 3 2022

      Presentation type：Poster presentation  

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    • 大腸菌ペプチドグリカン構築における新規調節因子SanAの機能解析

      山口 穂野香, 阿合 理沙, 田原 悠平, 笠井 大司, 宮田 真人, 塩見 大輔

      第16回日本ゲノム微生物学会年会（オンライン）  2 3 2022 

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      Event date： 2 3 2022 - 4 3 2022

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    • リアルタイム観察で明らかになってきた大腸菌L-formの増殖様式 Invited

      塩見大輔

      2021年日本細菌学会関東支部インターラボセミナー（オンライン）  21 10 2021 

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      Event date： 21 10 2021

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    • 細胞壁を持たない不定形な大腸菌L-formにおける染色体分配様式

      林匡史, 浪川結衣, 大島拓, 塩見大輔

      第93回日本遺伝学会（オンライン）  9 9 2021 

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      Presentation type：Oral presentation (general)  

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    • 大腸菌のバンコマイシン耐性関連因子SanAの機能解析

      山口穂野香, 阿合理沙, 塩見大輔

      第15回細菌学若手コロッセウム（オンライン）  30 8 2021 

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    • 桿菌・L-form間の分裂様式の返還と分裂装置の制御

      林匡史, 大島拓, 塩見大輔

      第15回細菌学若手コロッセウム（オンライン）  30 8 2021 

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    • 大腸菌L-formにおける代謝の変化 ~ L-form細胞におけるArcABとFnrの役割 ~

      伊藤わかな, 塩見大輔, 大島拓

      第17回21世紀大腸菌研究会（オンライン）  20 8 2021 

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      Event date： 20 8 2021

      Presentation type：Poster presentation  

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    • ペニシリン結合タンパク質の機能に対するSanAの影響

      山口穂野香, 阿合理沙, 塩見大輔

      第17回21世紀大腸菌研究会（オンライン）  20 8 2021 

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    • 細胞壁を持たないL-formにおける分裂装置の制御メカニズム

      林匡史, 大島拓, 塩見大輔

      第17回21世紀大腸菌研究会（オンライン）  20 8 2021 

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    • 細胞壁のない細菌が持つFtsZタンパク質の重合能解析

      笠井大司, 田原悠平, 宮田真人, 塩見大輔

      第17回21世紀大腸菌研究会（オンライン）  20 8 2021 

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    • 大腸菌L-formにおけるゲノムDNA維持機構の解析

      浪川結衣, 大島拓, 塩見大輔

      第17回21世紀大腸菌研究会（オンライン）  20 8 2021 

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    • 大腸菌L-formにおける分裂装置の制御メカニズム

      林匡史, 塩見大輔

      第15回日本ゲノム微生物学会年会 （オンライン）  5 3 2021 

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    • SanAによる大腸菌の新規バンコマイシン耐性機構の解析

      山口穂野香, 阿合理沙, 塩見大輔

      第15回日本ゲノム微生物学会年会 （オンライン）  5 3 2021 

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    • 異常な細胞壁の再利用が大腸菌L-formに与える影響

      近田大基, 大島拓, 塩見大輔

      第15回日本ゲノム微生物学会年会 （オンライン）  5 3 2021 

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    • 細胞壁のない細菌の細胞分裂タンパク質の重合能の解析

      笠井大司, 田原悠平, 宮田真人, 塩見大輔

      第15回日本ゲノム微生物学会年会 （オンライン）  4 3 2021 

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    • 細胞壁のリサイクリングが細胞壁のない大腸菌L-formの増殖に及ぼす影響

      近田大基, 大島拓, 塩見大輔

      第103回日本細菌学会関東支部総会 （オンライン）  24 10 2020 

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    • 細胞壁を持たない細菌のチューブリンの解析

      笠井大司, 塩見大輔

      第58回日本生物物理学会年会 （オンライン）  16 9 2020 

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    • ペプチドグリカン層を持たないL型大腸菌の増殖に外膜は重要か？

      塩見大輔, 近田大基, 大島拓

      第14回日本ゲノム微生物学会年会（ウインクあいち）  6 3 2020 

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    • Outer membrane is required for proliferation of Escherichia coli L-form. Invited

      19 2 2020 

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      Presentation type：Symposium, workshop panel (nominated)  

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    • 細胞壁のない細菌の細胞分裂タンパク質の解析

      笠井大司, 塩見大輔

      第93回日本細菌学会総会（ウインクあいち）  19 2 2020 

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    • RodZ regulates assembly of Rod complex in Escherichia coli.

      19 2 2020 

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    • Cell shape determination by Rod complex in Escherichia coli Invited

      Daisuke Shiomi

      4 12 2019 

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      Presentation type：Symposium, workshop panel (nominated)  

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    • 細胞壁を持たないL型大腸菌の増殖機構

      塩見大輔

      遺伝研研究会「微生物における大規模ゲノム・代謝改変技術とその利用」（遺伝研）  23 11 2019 

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      Presentation type：Oral presentation (invited, special)  

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    • 大腸菌のL-form化における細胞壁リサイクリングの重要性

      近田大基, 大島拓, 塩見大輔

      第18回微生物研究会（立教大学）  9 11 2019 

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    • 大腸菌MreBアクチン動態における細胞膜流動性の重要性

      栗田恵輔, 塩見大輔

      第18回微生物研究会（立教大学）  9 11 2019 

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    • RodZが関与するRod複合体クラスター構築と細胞形態制御の機構解明

      阿合理沙, 岡本尚, 仁木宏典, 塩見大輔

      第18回微生物研究会（立教大学）  9 11 2019 

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    • 大腸菌RodZが担う細胞形態維持機構の解明

      阿合理沙, 岡本尚, 仁木宏典, 塩見大輔

      第13回細菌学若手コロッセウム（旬樹庵さんさ亭 宮城・蔵王）  18 8 2019 

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      Presentation type：Oral presentation (general)  

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    • Spiroplasma eriocheiris の細胞分裂タンパク質の機能解析

      笠井大司, 塩見大輔

      第13回細菌学若手コロッセウム（旬樹庵さんさ亭 宮城・蔵王）  18 8 2019 

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    • 細胞壁を持たない細菌の細胞分裂タンパク質の機能

      笠井大司, 塩見大輔

      第16回21世紀大腸菌研究会（琵琶湖ホテル）  29 5 2019 

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    • 異なる Mg2+濃度下における大腸菌 L-form 変換過程の解析

      近田大基, 金井友美, 大島 拓, 塩見大輔

      第16回21世紀大腸菌研究会（琵琶湖ホテル）  29 5 2019 

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    • Rod 複合体新規関連因子 SanA の機能解析

      阿合理沙, 岡本 尚, 仁木宏典, 塩見大輔

      第16回21世紀大腸菌研究会（琵琶湖ホテル）  29 5 2019 

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    • 細胞壁を持たないスパイロプラズマの分裂

      笠井大司, 塩見大輔

      第92回日本細菌学会総会（札幌コンベンションセンター）  23 4 2019 

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    • Control of cell shape by a transmembrane protein RodZ and phospholipids in Escherichia coli

      23 4 2019 

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      Presentation type：Symposium, workshop panel (nominated)  

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    • L型大腸菌への変換過程の可視化とその遺伝的基盤の解析

      近田大基, 金井友美, 大島拓, 塩見大輔

      単細胞生物における細胞装置の機能と連携（国立遺伝学研究所）  19 3 2019 

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      Event date： 18 3 2019 - 19 3 2019

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    • 大腸菌形態形成因子RodZの膜貫通領域の機能解明に向けた遺伝学的解析

      阿合理沙, 岡本尚, 仁木宏典, 塩見大輔

      日本ゲノム微生物学会年会要旨集  6 3 2019 

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    • 形態形成制御因子RodZタンパク質による効率的なZリング形成

      吉井佑介, 仁木宏典, 塩見大輔

      日本ゲノム微生物学会年会要旨集  6 3 2019 

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    • シロイヌナズナにおける葉緑体のダイナミクスと炭疽病菌応答への関与~植物と微生物の相互作用,侵略者から用心棒へ~

      入枝泰樹, 入枝泰樹, 高野義孝, 塩見大輔

      日本植物病理学会植物感染生理談話会論文集  21 8 2018 

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    • RodZタンパク質は細胞分裂面でMerBアクチンとFtsZチューブリンを協調させる

      吉井佑介, 阿合理沙, 仁木宏典, 塩見大輔

      日本ゲノム微生物学会年会要旨集  5 3 2018 

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    • 大腸菌のMreBアクチンの細胞内動態にリン脂質が与える影響の解析

      栗田恵輔, 加藤郁也, 塩見大輔, 仁木宏典

      日本ゲノム微生物学会年会要旨集  5 3 2018 

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    • 大腸菌形態形成制御因子MreBアクチンと膜タンパク質RodZの動態の制御

      栗田恵輔, 阿合理沙, 加藤郁也, 仁木宏典, 塩見大輔

      日本農芸化学会大会講演要旨集(Web)  5 3 2018 

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    • キメラタンパク質によるRodZ膜貫通領域の機能解明

      阿合理沙, 仁木宏典, 塩見大輔

      日本ゲノム微生物学会年会要旨集  3 2018 

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    • バクテリアアクチンとリン脂質による細胞極性制御

      川面拓真, 松本夏音, 加藤郁也, 金井友美, 仁木宏典, 塩見大輔

      日本ゲノム微生物学会年会要旨集  2017 

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    • 大腸菌MreBアクチンの細胞内局在の制御機構

      塩見大輔, 川面拓真, 松本夏音, 小島広樹, 加藤郁也, 金井友美, 仁木宏典

      日本細菌学雑誌(Web)  2017 

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    • バクテリアアクチンが制御する細胞極性

      川面拓真, 小島広樹, 仁木宏典, 塩見大輔

      日本ゲノム微生物学会年会要旨集  2016 

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    • 膜貫通型タンパク質RodZの膜直下配列の重要性の検討

      塩見大輔, 仁木宏典

      日本ゲノム微生物学会年会要旨集  2015 

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    • 大腸菌形態制御因子RodZの分裂面への局在とその意義

      塩見大輔, 仁木宏典

      日本ゲノム微生物学会年会要旨集  2013 

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    • 桿菌の形を決める新規の細胞骨格性タンパク質

      SHIOMI DAISUKE, SAKAI MASAKO, NIKI HIRONORI

      日本細菌学雑誌  20 2 2009 

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    • 3P348 Single-cell analysis of E.coli's polarity

      Ayano S, Inoue I, Shiomi D, Kawagishi I, Yasuda K

      Biophysics  19 10 2005 

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    • Subcellular localization of histidine kinases in Escherichia coli

      Yoshimoto M, Shiomi D, Homma M, Kawagishi I

      Biophysics  19 10 2005 

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    • 2P228 Subcellular localization and clustering of the redox sensor Aer of Escherichia coli

      Ohta N, Banno S, Obata Y, Shiomi D, Homma M, Kawagishi

      Biophysics  19 10 2005 

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    • 大腸菌走化性受容体のメチル化による極局性とクラスター内相互作用の制御

      KAWAGISHI IKURO, HONMA MICHIO, IRIE YASUKI, SAKANO SATOMI, SHIOMI DAISUKE

      日本細菌学雑誌  25 2 2005 

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    • コレラ菌 Vibrio cholerae の3組のCheシステムとネットワークの細胞内局性

      MOMOTAKE AKIHIRO, NISHIOKA NORIKO, HONMA MICHIO, KAWAGISHI IKURO, ITO YASUAKI, SHIOMI DAISUKE

      日本細菌学雑誌  25 2 2005 

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    • 3P213 Simultaneous measurement of dynamics of sensor-protein localization and motility behavior in individual Escherichia coli cells

      Inoue I, Shiomi D, Kawagishi I, Yasuda K

      Biophysics  10 11 2004 

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    • 2P144 Subcellular localization of the redox sensor Aer of Escherichia coli and its interaction with the chemoreceptor

      Obata Y, Shiomi D, Homma M, Kawagishi I

      Biophysics  10 11 2004 

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    • 2P143 Negative feedback through the localization control of the receptor methylesterase CheB in the bacterial chemotaxis

      Banno S, Shiomi D, Homma M, Kawagishi I

      Biophysics  10 11 2004 

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    • 2P142 Polar and helical localization of the chemoreceptor in an Escherichia coli cell

      Yoshimoto M, Shiomi D, Homma M, Kawagishi I

      Biophysics  10 11 2004 

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    • オンチップ1細胞培養系を用いた大腸菌内タンパク発現と細胞運動ダイナミクスの同時顕微鏡計測

      安田賢二, 井之上一平, 若本祐一, 梅原千慶, 川岸郁朗, 塩見大輔

      日本分子生物学会年会プログラム・講演要旨集  25 11 2003 

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    • オンチップ大腸菌―細胞培養系を用いた走化性レセプター局在ダイナミクスおよび細胞運動能の世代間比較計測

      井之上一平, 若本祐一, 塩見大輔, 川岸郁朗, 安田賢二

      日本分子生物学会年会プログラム・講演要旨集  25 11 2003 

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    • Measurement of sensor-protein dynamics in bacterial cytoplasm by use of the on-chip single cell observation system.

      Inoue I, Wakamoto Y, Shiomi D, Kawagishi I, Yasuda K

      Biophysics  25 8 2003 

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    • Does the aspartate chemoreceptor Tar amplify signals through its interdimer interaction?

      Homma M, Shiomi D, Homma M, Kawagishi I

      Biophysics  25 8 2003 

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    • The recognition of the chemotactic receptor-kinase complex by the methylesterase CheB.

      Banno S, Shiomi D, Homma M, Kawagishi I

      Biophysics  25 8 2003 

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    • Subcellular localization of the Aer in redox taxis of Escherichia coli.

      Obata Y, Shiomi D, Homma M, Kawagishi I

      Biophysics  25 8 2003 

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    • Mechanism of targeting of the bacterial chemoreceptor to a cell pole.

      Shiomi D, Yoshimoto M, Irieda H, Homma M, Kawagishi I

      Biophysics  25 8 2003 

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    • 大腸菌走化性レセプターのダイマー間相互作用に対するメチル化と誘引物質の影響

      本間幹啓, 塩見大輔, 本間道夫, 川岸郁朗

      日本生物物理学会年会講演予稿集  11 2002 

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    • 大腸菌走化性に関与する脱メチル化酵素CheBの細胞内局在の解析

      坂野聡美, 塩見大輔, 本間道夫, 川岸郁朗

      日本生物物理学会年会講演予稿集  11 2002 

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    • 大腸菌細胞極における走化性レセプター・キナーゼ複合体形成の制御機構

      塩見大輔, 本間道夫, 川岸郁朗

      日本生物物理学会年会講演予稿集  11 2002 

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    • 1C900 Regulation of the bacterial chemoreceptor-kinase complex at cell poles.

      Shiomi D, Homma M, Kawagishi I

      Biophysics  10 10 2002 

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    • 1C0915 Polar localization of the chemotactic methylesterase CheB of Escherichia coli

      Banno S, Shiomi D, Homma M, Kawagishi I

      Biophysics  10 10 2002 

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    • 1C0930 Effects of the methylation and the attractant on the interdimer interaction of the chemoreceptor of Escherichia coli

      Homma M, Shiomi D, Homma M, Kawagishi I

      Biophysics  10 10 2002 

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    • 1C1000 Analysis of the three homologs of the methltransferase CheR in Vibrio cholerae

      Hyakutake A, Nishioka N, Shiomi D, Homma M, Kawagishi I

      Biophysics  10 10 2002 

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    • 大腸菌アスパラギン酸レセプターのクラスター形成とシグナル伝達

      本間幹啓, 塩見大輔, 本間道夫, 川岸郁朗

      生化学  25 8 2002 

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    • 大腸菌走化性レセプターの極局在化機構

      塩見大輔, 小幡裕美, 本間道夫, 川岸郁朗

      生化学  25 8 2002 

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    • 大腸菌走化性の適応過程におけるシグナル伝達タンパク質の細胞内局在

      塩見大輔, ZHULIN I, 本間道夫, 川岸郁朗

      日本生物物理学会年会講演予稿集  10 2001 

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    • Effect of methylation of the chemoreceptor on its ligand-binding affinity and subcellular localization

      Sakamoto H, Shiomi D, Iwama T, Homma M, Kawagishi I

      Biophysics  10 9 2001 

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    • Subcellular localization of signaling proteins in adaptation of E.coli chemotaxis

      Shiomi D, Igor Zhulin, Homma M, Kawagishi I

      Biophysics  10 9 2001 

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    • 大腸菌走化性に関与するタンパク質メチル化酵素による走化性レセプター認識機構

      塩見大輔, ZHULIN I B, 本間道夫, 川岸郁朗

      生化学  25 8 2001 

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    • 大腸菌走化性における膜貫通型レセプターとメチル化酵素の相互作用

      塩見大輔, ZHULIN I B, 本間道夫, 川岸郁朗

      日本遺伝学会大会プログラム・予稿集  22 8 2001 

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    • Functional analysis of the bacterial methyltransferase CheR involved in chemotactic adaptation.

      Shiomi D, Zhulin Igor, Homma M, Kawagishi I

      Biophysics  5 8 2000 

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    • 細菌走化性レセプターとメチル基転移酵素の相互作用とその適応における役割

      SHIOMI DAISUKE, FURIHATA TATSUYA, SATO KEN, HONMA MICHIO, KAWAGISHI IKURO

      日本生物物理学会年会講演予稿集  2 9 1999 

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    • Interaction between the bacterial chemoreceptor Tar and the methyltransferase CheR and its role in chemotactic adaptation

      Shiomi D, Furihata T, Sato K, Homma M, Kawagishi I

      Biophysics  2 9 1999 

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    • Mutational analysis of the methyltransferase-binding sequence of the bacterial chemoreceptor, which is critical for chemotactic adaptation

      SHIOMI Daisuke, OKUMURA Hisashi, HOMMA Michio, KAWAGISHI Ikuro

      The Japanese journal of taste and smell research  1 12 1998 

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    • Mutational analysis of the carboxy-terminal sequence of the chemoreceptor that serves as the binding site for methyltransferase CheR

      Shiomi D, Okumura H, Homma M, Kawagishi I

      Biophysics  7 9 1998 

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    Professional Memberships

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      日本ゲノム微生物学会

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      JAPANESE SOCIETY FOR BACTERIOLOGY

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    Research Projects

    • ペプチドグリカンを失った大腸菌L-formの増殖機構の解明

      日本学術振興会  科学研究費助成事業 

      塩見 大輔

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      4 2024 - 3 2027

      Grant number：24K01673

      Grant amount：\18460000 （ Direct Cost: \14200000 、 Indirect Cost：\4260000 ）

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    • 合成細菌JCVI syn3.0B とゲノム操作を用いた細胞進化モデルの構築

      科学技術振興機構  CREST 

      宮田 真人, 研究者, 塩見 大輔

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      10 2019 - 3 2025

      Authorship：Principal investigator  Grant type：Competitive

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    • Regulatory mechanisms of bacterial morphology by cytoskeletal proteins.

      Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research 

      SHIOMI Daisuke

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      2015 - 2017

      Grant number：15H04731

      Authorship：Principal investigator  Grant type：Competitive

      Grant amount：\9230000 （ Direct Cost: \7100000 、 Indirect Cost：\2130000 ）

      Bacterial cell shape is regulated by cytoskeletal proteins which are homologs of eukaryotic cytoskeletal proteins. In this study, we analyzed functions and subcellular localizations of MreB actin and its regulator protein RodZ. We found that compositions of phospholipids are important for subcellular localizations and motions of MreB. We also showed that RodZ self-interacts in the periplasmic domain. In addition, the transmembrane region of RodZ is vital for its function. We published two papers and a review in international scientific journals. We are now preparing one more paper to publish.

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    • バクテリア形態形成を制御する複合体の動態と機能解析

      文部科学省  科学研究費補助金(新学術領域研究(研究領域提案型)) 

      塩見 大輔

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      2015 - 2016

      Grant number：15H01333

      Authorship：Principal investigator  Grant type：Competitive

      Grant amount：\5850000 （ Direct Cost: \4500000 、 Indirect Cost：\1350000 ）

      1. MreB,RodZタンパク質の細胞内動態解析 本年度はMreB-mCherryまたはGFP-RodZを発現する形態異常株においてこれらのタンパク質の動態を顕微鏡で観察することを計画した。細胞幅が細い変異株や太い変異株を用いて、それらの株におけるMreB-mCherryの動態を調べた。その結果、野生株に比べて細い株ではMreBは速く運動し、逆に、太い株ではMreBは野生株よりも遅く運動することを明らかにした。また、これらの株では一細胞当たりのペプチドグリカン量は変わらなかった。MreBの運動能の違いがペプチドグリカンの構造の違いを生み出し、その結果、細胞幅が異なるのかもしれない。
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      2. MreB複合体形成機構 MreBは細胞内で長いフィラメントを形成するという報告と、短いフィラメントあるいはクラスターを形成するという２つの相反する結果が報告されている。実際に、我々の研究室でも、MreBがどちらの状態も取り得ることを観察した。この原因を探るため、個々の細胞のMreBの発現量とMreBの局在を同時に観察する系を構築した。mreBプロモーターの制御下でgfpを発現するプラスミドを構築し、そのプラスミドをMreB-mCherryを発現する株に導入した。この株でGFPとmCherryの発現を同時観察した。その結果、MreBの発現量と局在のパターンに明確な相関は見出されなかった。次に、個々の細胞でのATP濃度の違いがMreBの局在パターンに違いをもたらしている可能性を考えた。ATP濃度はQUEENタンパク質で可視化することを試みた。残念ながら、本年度ではQUEENタンパク質を用いたATP濃度の可視化に成功しなかった。ATP濃度とMreBの局在パターンの関係の解析は今後も継続する予定である。

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    • バクテリア細胞骨格タンパク質複合体の構築と制御機構の解析

      文部科学省  科学研究費補助金(新学術領域研究(研究領域提案型)) 

      塩見 大輔

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      2013 - 2014

      Grant number：25117528

      Authorship：Principal investigator  Grant type：Competitive

      Grant amount：\10010000 （ Direct Cost: \7700000 、 Indirect Cost：\2310000 ）

      大腸菌のような桿菌の形態を正しく形成するためには、細胞の短軸方向に沿って回転運動をするバクテリアアクチンMreBが必須である。MreBの重合を含めた機能発現にはその制御因子であるRodZが重要な役割を果たす。そこで、この形態形成に重要な回転する超分子複合体の機能や運動のメカニズムを明らかにするために、再構成系の構築を始めた。好熱菌Thermotoga martimaからMreBおよびRodZを精製した。MreBをAlexa488で標識し、これをリポソームに封入した。予備実験の段階ではあるが、MreBは膜に取り込まれた。そして、リポソーム内で膜全体に広がるもの、クラスターを形成するものが観察された。またRodZも同時に封入した場合、フィラメント様の構造も観察された。また、生体内でこの複合体を構成するタンパク質間相互作用を解析する光架橋実験系を立ち上げた。この実験系により、RodZタンパク質はペリプラズム領域で複数のタンパク質と相互作用することが明らかとなった。このようなタンパク質間相互作用と複合体の動態の関係の解析は今後の課題である。RodZタンパク質の解析も行った。膜タンパク質であるRodZは、膜直下に正電荷を持つアミノ酸を多く持つ。この領域にある正電荷をもつアミノ酸全てをアラニンに置換したが、RodZの機能に影響しなかった。したがって、正電荷は機能に関係しない。また、この領域をMalFタンパク質の細胞質領域と置き換えた。その結果、この領域のアミノ酸配列が必要なのではなく、領域の長さが必要であることが分かった。したがって、ある程度の長さを必要とするリンカーのような役割をしていることが推測された。

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    • Analyses of molecular mechanisms of regulation of bacterial shape by cytoskeletal protein complex.

      Ministry of Education, Culture, Sports, Science and Technology  Grants-in-Aid for Scientific Research(若手研究(B)) 

      Daisuke SHIOMI

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      2012 - 2013

      Grant number：24770191

      Authorship：Principal investigator  Grant type：Competitive

      Grant amount：\4550000 （ Direct Cost: \3500000 、 Indirect Cost：\1050000 ）

      Purpose of this project was to understand molecular mechanism to regulate bacterial cell shape. Analyses of the suppressor mutants of the rodZ mutant suggested that RodZ regulates assembly of MreB filaments. This result was published in 2012. In order to analyze the importance of the positively-charged residues in the juxta-membrane domain, I introduced Alanine into the residues and deleted the domain. I found that the positively-charged residues is dispensable for the RodZ function while the length of the domain is critical. I also analyzes the interaction among proteins constituting supramolecular machinery, elongasome. I found that RodZ interacts with MreB, MreC, PBP2, and RodA and that there are two sub-complexes in the complex, that is, MreB/MreC and PBP2/RodA complexes. The results indicate that RodZ bridges the sub-complexes. I also applied site-specific in vivo photo crosslink assay to detect interaction between RodZ and other proteins. I could detect crosslinked products.

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    • Analysis of a mechanism of regulation of bacterial cell shape by a novel protein RodZ

      Ministry of Education, Culture, Sports, Science and Technology  Grants-in-Aid for Scientific Research(若手研究(B)) 

      Daisuke SHIOMI

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      2010 - 2011

      Grant number：22770179

      Authorship：Principal investigator  Grant type：Competitive

      Grant amount：\4290000 （ Direct Cost: \3300000 、 Indirect Cost：\990000 ）

      I have shown that a novel protein RodZ colocalizes with MreB, a bacterial actin, and forms spirals along the long axis of the cell. Thus, we think that RodZ along with MreB regulates the cell length. I found in this study that RodZ localizes at midcell dependently on MreB and FtsZ, a bacterial tubulin. Cells producing RodZ which cannot localize at midcell are wider that cells producing WT RodZ, suggesting that RodZ regulates the cell width as well as the cell length.

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    • Analyses of a novel cell shape determinant in rod-shaped bacterium Escherichia coli.

      Ministry of Education, Culture, Sports, Science and Technology  Grants-in-Aid for Scientific Research(若手研究(スタートアップ)) 

      Daisuke SHIOMI

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      2008 - 2009

      Grant number：20870039

      Authorship：Principal investigator  Grant type：Competitive

      Grant amount：\3302000 （ Direct Cost: \2540000 、 Indirect Cost：\762000 ）

      I identified a novel cytoskeletal membrane protein RodZ which regulates cell shape in rod-shaped bacterium E.coli. Cells lacking rodZ are round. It was suggested that RodZ regulates the cell length. Analyses of suppressor mutants of cells lacking rodZ revealed genetic interactions between RodZ and MreB (actin) or cell division machinery that includes FtsZ (tubulin), suggesting that all three cytoskeletal proteins in E.coli collaborate to determine cell shape.

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    • 大腸菌走化性におけるタンパク質間相互作用のダイナミクス

      日本学術振興会  科学研究費助成事業 

      塩見 大輔

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      2002 - 2003

      Grant number：02J05478

      Grant amount：\2000000 （ Direct Cost: \2000000 ）

      多くの感覚応答系において、入力されたシグナルの増幅は必須である。大腸菌走化性においても、走化性レセプター(MCP)がシグナルタンパク質(CheA,CheWなど)と菌体の極で複合体を形成しており、この極複合体内でのMCPダイマー間の相互作用がシグナル増幅を引き起こすと考えられている。我々は、アスパラギン酸レセプターTarのペリプラズム領域に2つのシステイン残基(サブユニット界面とダイマー間)を導入し、Tarダイマー間の相互作用を調べた。我々は、架橋されたTarが推定6量体を形成することを明らかにした。これはセリンレセプターTsrの細胞質断片の結晶が6量体ユニットを形成することと一致する。また、この推定6量体が誘引物質(アスパラギン酸)の添加により減少した。しかし、アスパラギン酸の添加はTar-GFPの極局在に大きく影響しなかった。つまり、誘引物質の添加により、ダイマー間の相互作用が変化したことが分かる。このようなMCPダイマー間相互作用の変化がシグナル増幅に関与しているかもしれない。
      これまでに、MCPが極に局在していることは明らかになっているが、この極局在がなんらかの制御を受けているかは明らかでない。MCPはCheR,CheBによりメチル化、脱メチル化修飾を受ける。これらの酵素の極局在がMCPのメチル化に依存していることが分かった。これは、これらの標的であるMCPの局在が自身のメチル化に制御されている可能性を示唆している。Tar-GFPのメチル化レベルを変えてTar-GFPの極局在を観察したところ、確かにメチル化レベルが高いほどTar-GFPはより極へ局在した。これは、CheA,CheWがないときにより顕著に観察された。またCheA,CheWがないときに忌避物質を加えると、Tarはクラスターを形成した。このことは、Tar-GFPの極局在がわずかながらもリガンドに制御されていることを示している。また、脱メチル化型Tar-GFPとTsrを共発現させるとTar-GFPの極局在が促進された。このことは、異種レセプターダイマー間で複合体を形成し、極に局在していることを示している。 (一部投稿準備中)

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