2014 Fiscal Year Final Research Report
Elucidation of the directional switching mechanism of the bacterial flagellar motor
Project/Area Number |
24570131
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Osaka University |
Principal Investigator |
MIYATA Tomoko 大阪大学, 生命機能研究科, 特任助教(常勤) (30423156)
|
Co-Investigator(Renkei-kenkyūsha) |
MATSUNAMI Hideyuki 沖縄科学技術大学院大学, 細胞膜通過輸送研究ユニット, 研究員 (80444511)
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Project Period (FY) |
2012-04-01 – 2015-03-31
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Keywords | 単粒子解析 / 電子顕微鏡 / 分子モーター |
Outline of Final Research Achievements |
Many bacteria swim by reversibly rotating flagella. The switch complex consists of three switch proteins, FliG, FliM and FliN which control counter clockwise-clockwise (CCW/CW) switching of the motor rotation, form the C-ring on the cytoplasmic face of the MS ring. CheY is a response regulator in bacterial chemotaxis, and phosphorylated CheY (CheY-p) binds to FliM and changes the rotational direction from CCW to CW. We report the C ring structures locked in CCW (che deletion strain) and CW (FliG ΔPAA strain). Comparison of the two strucures showed differences in the position of the C ring and the subunit arrangement in its outer wall. FliM and FliN were well fitted into the middle and lower parts of the outer ring of the C-ring, but the location of FliG remains uncertain. We report the FliG labelling experiments and the structure analysis of the CheY-p bound C ring by electron cryomicroscopy.
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Free Research Field |
構造生物学
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