2012 Fiscal Year Final Research Report
Molecular mechanism of the assembly and disassembly processes of the bacterial flagellum-specific ATPase complex
Project/Area Number |
22570161
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | Osaka University |
Principal Investigator |
MINAMINO Tohru 大阪大学, 生命機能研究科, 准教授 (20402993)
|
Research Collaborator |
KINOSHITA Miki 大阪大学, 生命機能研究科, 特任研究員
MORIMOTO Yusuke 大阪大学, 生命機能研究科, 特任研究員
HARA Noritaka 大阪大学, 生命機能研究科, 大学院生
|
Project Period (FY) |
2010 – 2012
|
Keywords | 電子顕微鏡 / 分子モーター / 遺伝学 / 細菌 / 蛋白質 |
Research Abstract |
The bacterial flagellar ATPase complexes, which consist of FliH, FliI and FliJ, associate with the docking platform of the export gate through an interaction between FliH and an export gate protein FlhA, thereby forming the FliI6-FliJ ring complex. A specific interaction of FliJ with FlhA brought about by the FliHX-FliI_6 complex allows the export gate to fully utilize proton motive force across the cytoplasmic membrane to drive flagellar protein export.
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[Journal Article] Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus2013
Author(s)
Ibuki, T., Uchida, Y., Hironaka, Y., Namba, K., Imada, K., Minamino, T.
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Journal Title
J. Bacteriol.
Volume: 195
Pages: 466-473
Peer Reviewed
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[Journal Article] Interaction of a bacterial flagellar chaperone FlgN with FlhA is required for efficient export of its cognate substrates.2012
Author(s)
Minamino, T., Kinoshita, M., Hara, N., Takeuchi, S., Hida, A., Koya, S., Glenwright, H., Imada, K., Aldridge, P.D., & Namba, K
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Journal Title
Mol. Microbiol.
Volume: 83
Pages: 775-788
Peer Reviewed
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[Journal Article] Common architecture between the flagellar type III protein export apparatus and F- and V-type ATPases2011
Author(s)
Ibuki, T., Imada, K., Minamino, T., Kato, T., Mitata, T., Namba, K
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Journal Title
Nat. Struct. Mol. Biol.
Volume: 18
Pages: 277-282
Peer Reviewed
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