| Project Area | Innovative nanoscience of supermolecular motor proteins working in biomembranes |
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| 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 |
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| Review Section |
Biological Sciences
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| Research Institution | Nagoya University |
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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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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥163,400,000 (Direct Cost: ¥163,400,000)
Fiscal Year 2010: ¥28,600,000 (Direct Cost: ¥28,600,000)
Fiscal Year 2009: ¥34,600,000 (Direct Cost: ¥34,600,000)
Fiscal Year 2008: ¥34,700,000 (Direct Cost: ¥34,700,000)
Fiscal Year 2007: ¥34,600,000 (Direct Cost: ¥34,600,000)
Fiscal Year 2006: ¥30,900,000 (Direct Cost: ¥30,900,000)
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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 |
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| 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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