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)
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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)
|
Project Period (FY) |
2012-04-01 – 2015-03-31
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Project Status |
Completed (Fiscal Year 2014)
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Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2014: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
|
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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Report
(4 results)
Research Products
(22 results)
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[Journal Article] Common and distinct structural features of Salmonella injectisome and flagellar basal body2013
Author(s)
Kawamoto, A., Morimoto, Y.V., Miyata, T., Minamino, T., Hughes, K.T., Kato, T. & Namba, K.
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Journal Title
Scientific Reports
Volume: 3
Issue: 1
Pages: 3369-3369
DOI
Related Report
Peer Reviewed
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[Journal Article] A method to achieve homogeneous dispersion of large transmembrane complexes within the holes of carbon films for electron cryomicroscopy.2013
Author(s)
Cheung, M., Kajimura, N., Makino, F., Ashihara, M., Miyata, T., Kato, T., Namba, K., Blocker, A. J.
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Journal Title
J. Struct. Biol.
Volume: 182(1)
Pages: 51-60
Related Report
Peer Reviewed
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[Presentation] Functional analysis of the bacterial flagellar motor in fliFG fusion mutants.2014
Author(s)
Mori, K., Hiraoka, K., Morimoto, Y.V., Miyata, T., Kami-ike, N., Minamino, T., Namba, K.
Organizer
GRC on Sensory Transduction in Microorganisms
Place of Presentation
Ventura Beach Marriott (USA)
Related Report
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[Presentation] Structural analysis of the flagellar hook-basal body with the C ring by electron cryomicroscopy.2013
Author(s)
Miyata, T., Kato, T., Fujii, T., Nakamura, S., Morimoto, Y.V., Minamino, T., Matsunami, H. and Namba, K.
Organizer
Nagoya Symposium -Frontiers in Structural Physiology
Place of Presentation
Nagoya University
Related Report
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[Presentation] 細菌べん毛モーターの回転方向変換制御機構の解明.Elucidation of the directional switching mechanism of the bacterial flagellar motor.2012
Author(s)
Miyata, T., Kato, T., Fujii, T., Nakamura, S., Morimoto, Y., Minamino, T., Matsunami, H., Namba, K.
Organizer
第50回日本生物物理学会年会
Place of Presentation
名古屋大学(愛知県)
Related Report
Invited
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[Presentation] Common and distinct structural features of Salmonella injectisome and flagellar basal body.
Author(s)
Kawamoto, A., Morimoto, Y.V., Miyata, T., Minamino, T., Hughes, K.T., Kato, T., Namba, K.
Organizer
GRC on Sensory Transduction in Microorganisms
Place of Presentation
Ventura Beach Marriott (USA)
Related Report
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