| Project/Area Number |
13308037
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
FUTAI Masamitu Osaka University, Professor, 産業科学研究所, 教授 (50012646)
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| Co-Investigator(Kenkyū-buntansha) |
WADA Yoh Osaka University, Associate Professor, 産業科学研究所, 助教授 (50212329)
SUN-WADA Ge-hong Osaka University, Assistant Professor, 産業科学研究所, 助手 (00314427)
三本木 至宏 大阪大学, 産業科学研究所, 助手 (10222027)
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| Project Period (FY) |
2001 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥27,040,000 (Direct Cost: ¥20,800,000、Indirect Cost: ¥6,240,000)
Fiscal Year 2003: ¥14,430,000 (Direct Cost: ¥11,100,000、Indirect Cost: ¥3,330,000)
Fiscal Year 2002: ¥12,610,000 (Direct Cost: ¥9,700,000、Indirect Cost: ¥2,910,000)
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| Keywords | ATP / ATP sypthase / Rotation / F-type ATPase / V-type ATPase / lysosomes / プロトンポンプ / H^+-ATPase / 回転触媒 / エネルギー共益 / 分子モーター / 膜輸送 / F-ATPase / V-ATPase / ATPase合成酵素 / F_0F_1 |
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| Research Abstract |
ATP synthase (F-type ATPase) synthesizes most of ATP required for plants or animals. We have shown that ATP synthase couples chemical reaction and proton transport through subunit rotation. Thus, this enzyme can be defined as a nanomotor generating biological energy currency. We have purified ATP synthase or prepared planar membranes from E..coli, and immobilized them on glass surface through a His-tag introduced into the c subunit or α subunit. Upon addition of ATP, an action filament connected to the α β or c subunit of ATP synthase (purified or in membrane) rotated continuously to the anti-clock wise direction. These results were extended to the studies of the rotation mechanism.
The vacuolar type ATPase (V-ATPase) is similar to the ATP synthase. We could also show that this proton pump carries out subunit rotation during catalysis. V-ATPase is localized in endomembrane organelles such as lysosomes, synaptic vesicles and endsosomes. We found the diverse subunit organization of this proton pump, depending on its location.
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