Molecular clutch between ATP and proton motors in ATP synthase
| Project/Area Number |
15K07013
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Rikkyo University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2018: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2017: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
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| Keywords | 生体エネルギー変換 / 共役 / 活性調節 / 脱共役 / ATP / プロトン輸送 / 酸化的リン酸化 / 律速 / アロステリック / 調節 / 架橋 / ヌクレオチド結合 |
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| Outline of Final Research Achievements |
(1)It was shown that inter-subunit interactions within rotor components is altered under uncoupling state. (2)Recovery of the coupling by the inter-subunit cross-linking has not been observed so far. (3)It was shown that one third of the TFoF1 molecules may be incomplete.(4) A mutant epsilon subunit with higher affinity for ATP was obtained. (5) The physiological significance of the regulation of ATP synthase in Bacillus subtilis was clarified.
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| Academic Significance and Societal Importance of the Research Achievements |
いまだ不明な点の多い、ATP合成酵素の条件的脱共役状態について、さまざまな知見を得ることができた。更に研究を続け分子機構の解明へとつなげたい。
ATP合成酵素の活性調節機構は原核生物と真核生物では異なるため、抗生物質の作用点として注目されている。条件的脱共役も、εサブユニットが構造変化をするバクテリアATP合成酵素のみが持つ性質であると考えられることから、同様に全く新しい抗生物質の作用点として活用することも期待される。
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Report
(6 results)
Research Products
(18 results)
