| Project/Area Number |
16K21472
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional biochemistry
Biophysics
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| Research Institution | Kyoto Sangyo University |
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Principal Investigator |
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| Research Collaborator |
MITSUOKA Kaoru
UCHIHASHI Takayuki
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | 6 量体 ATPase / V-ATPase / 回転分子モーター / 単粒子解析 / 1分子観察 / 電子顕微鏡 / 低温電子顕微鏡 / 6量体 ATPase / AAA+-ATPase / ６量体ATPase / 高速原子間力顕微鏡 |
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| Outline of Final Research Achievements |
Hexametric ATPases, like AAA+-ATPase, play important roles in cell. The conformational changes of hexametric ATPases associated with ATP hydrolysis is essential for its function. However, the mechanisms of the conformational changes are remains unknown. In this study, I attempted to reveal the mechanism by single-molecule-analysis (SPA) using cryogenic electron microscopy and single molecule direct observation technique.
I solved three structures of V-ATPase, a kind of hexametric ATPase, by SPA. From this result, the catalytic mechanism of V-ATPase was partially revealed. In addition, to investigate the interaction between hexametric ATPase and its substrate, I designed artificial substrate and measured the interaction. As the result, it is strongly indicated that the interaction among them is rough rather than specific and robust.
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