Structural and functional analyses of a core complex of the bacterial flagellar export gate complex
Project/Area Number |
18K14638
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Research Category |
Grant-in-Aid for Early-Career Scientists
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Allocation Type | Multi-year Fund |
Review Section |
Basic Section 43020:Structural biochemistry-related
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Research Institution | Osaka University |
Principal Investigator |
Kinoshita Miki 大阪大学, 生命機能研究科, 特任研究員(常勤) (30790985)
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Project Period (FY) |
2018-04-01 – 2020-03-31
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Project Status |
Completed (Fiscal Year 2019)
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Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2019: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2018: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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Keywords | 細菌 / 蛋白質 / 遺伝学 / 電子顕微鏡 / 感染症 |
Outline of Final Research Achievements |
The bacterial flagellar export gate complex is composed of five membrane proteins, FlhA, FlhB, FliP, FliQ and FliR, and utilizes proton motive force across the cytoplasmic membrane as the energy source to drive flagellar protein export. In this study, I investigated how the protein export channel of the export gate complex is opened to allow export substrates to cross the cytoplasmic membrane. I have provided experimental evidence suggesting that the C-terminal cytoplasmic domains of FlhA and FlhB not only mediates a hierarchical protein targeting but also regulate gate opening of the FliPQR protein export channel complex.
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Academic Significance and Societal Importance of the Research Achievements |
腸管出血性病原性大腸菌O157などの病原細菌による感染症は社会問題の一つで、それらの感染機構の解明ならびに克服のための方法の探索が続けられている。べん毛タンパク質輸送装置と高い相同性を示すIII型分泌装置が急性胃腸炎の発症に深く関わっている。本研究成果に基づいて病原性細菌のIII型分泌装置のゲート開閉機構を特異的に不活性化できれば、病原性細菌の病原性のみを破壊できる。したがって、従来の抗生物質のように細菌を死滅させることがないため耐性菌が発生しづらく、感染症の予防を含めた、これまでにない新しい治療法の開発につながると期待できる。
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Report
(3 results)
Research Products
(21 results)
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[Journal Article] Structural insights into the substrate specificity switch mechanism of the type III protein export apparatus2019
Author(s)
Y., Y. Ogawa, M. Kinoshita, N. Terahara, M. Shimada, N. Kodera, T. Ando, K. Namba, A. Kitao, K. Imada, T. Minamino
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Journal Title
Structure
Volume: 印刷中
Issue: 6
Pages: 965-976
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Structural insight into the substrate specificity switching mechanism of the type III protein export apparatus2019
Author(s)
Inoue Y, Ogawa Y, Kinoshita M, Terahara N, Shimada M, Kodera N, Ando T, Namba K, Kitao A, Imada K, Minamino T
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Journal Title
Related Report
Peer Reviewed / Open Access
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