2010 Fiscal Year Final Research Report
Study on the mechanism of force generation in the sodium-driven flagellar motor
Project Area | Innovative nanoscience of supermolecular motor proteins working in biomembranes |
Project/Area Number |
18074003
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Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
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Allocation Type | Single-year Grants |
Review Section |
Biological Sciences
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Research Institution | Nagoya University |
Principal Investigator |
HOMMA Michio Nagoya University, 理学研究科, 教授 (50209342)
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Co-Investigator(Kenkyū-buntansha) |
KOJIMA Seiji 名古屋大学, 大学院・理学研究科, 助教 (70420362)
KOJIMA Seiji 名古屋大学, 大学院・理学研究科, 助教 (20262842)
KAKINUMA Yohimi 愛媛大学, 農学部, 教授 (80134394)
MURATA Takeshi 千葉大学, 大学院・理学研究科, 特任准教授 (80415322)
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Co-Investigator(Renkei-kenkyūsha) |
KOJIMA Seiji 名古屋大学, 大学院・理学研究科, 助教 (20262842)
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Project Period (FY) |
2006 – 2010
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Keywords | モーター / ナノテク / ナトリウムイオン / 生体エネルギー / べん毛 |
Research Abstract |
The bacterial flagellar motor is a molecular machine powered by an electrochemical potential gradient of ions across the cytoplasmic membrane. The marine bacterium Vibrio alginolyticus has a single polar flagellum that enables it to swim in liquid by Na^+ ions. Until this study, the ion flux pathway in the stator complex is almost unknown. We experimentally showed that Na^+ ions bind to PomB-24 by ATR-FTIR. Furthermore, the ion pathway was inferred by the mutations of the transmembrane regions of stator proteins. Next, we investigated the localization of the GFP-fused stator complex and we found that the stator is assembled into a functional motor around the rotor only in the presence of Na+ ions. Furthermore, we determined the crystal structure of a C-terminal periplasmic fragment of a stator protein and we could suggest that drastic conformational changes in the N-terminal portion of the stator protein are required both for PG binding and the ion channel activation.
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Research Products
(66 results)
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[Journal Article] The significance of a glutamate-139 residue of V-type Na+-ATPase NtpK subunit in its catalytic turnover linked with salt tolerance of Enterococcus hirae.2011
Author(s)
Kawano-Kawada, M., Takahashi, H., Igarashi, K, Murata, T., Yamato, I, Homma, M., Kakinuma, Y.
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Journal Title
Peer Reviewed
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[Journal Article] Interaction between Na+ ion and carboxylates of the PomA-PomB stator unit studied by ATR-FTIR spectroscopy.2009
Author(s)
Sudo, Y., Kitade, Y., Furutani, Y., Kojima, M., Kojima, S., Homma, M., Kandori, H.
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Journal Title
Biochemistry. 48(49)
Pages: 11699-11705
Peer Reviewed
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[Journal Article] Stator assembly and activation mechanism of the flagellar motor by the periplasmic region of MotB.2009
Author(s)
Kojima, S., Imada, K., Sakuma, M., Sudo, Y., Kojima, C., Minamino, T., Homma, M., Namba, K.
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Journal Title
Mol.Microbiol. 73(4)
Pages: 710-718
Peer Reviewed
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[Journal Article] Torque-speed relationships of Na+-driven chimeric flagellar motors in Escherichia coli.2008
Author(s)
Inoue, Y., Lo, C.J., Fukuoka, H., Takahashi, H., Sowa, Y., Pilizota, T., Wadhams, G.H., Homma, M., Berry, R.M., Ishijima, A.
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Journal Title
J.Mol.Biol. 376(5)
Pages: 1251-1259
Peer Reviewed
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[Journal Article] Electron cryomicroscopic visualization of PomA/B stator units of the sodium-driven flagellar motor in liposomes.2006
Author(s)
Yonekura, K., Yakushi, T., Atsumi, T., Maki-Yonekura, S., Homma, M., Namba, K.
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Journal Title
J.Mol.Biol. 357
Pages: 73-81
Peer Reviewed
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