2005 Fiscal Year Final Research Report Summary
Proton pump ATPase as nano motors
| Project/Area Number |
13142204
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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 | Microbial Chemistry Research Center (2004-2005)
Osaka University (2001-2003) |
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Principal Investigator |
FUTAI Masamistu Microbial Chemistry Research Center, Futai Special Laboratory, Special Researcher, 微生物化学研究センター・二井特別研究室, 特別研究員 (50012646)
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| Co-Investigator(Kenkyū-buntansha) |
SUN-WADA Ge-hong Doshisya Womens' College pharmaceutical, Assistant Professor, 薬学部, 助教授 (00314427)
TAKAZAWA Shinn Tohoku University, Graduate School of Medicine, Assistant Professor, 医科学系研究科, 助教授 (50187944)
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| Project Period (FY) |
2001 – 2005
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| Keywords | ATP / F-TPase / V-ATPase / Lisosom / nano machine / nano motors |
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| Research Abstract |
Three classes of proton pumping ATPase are known : P-TPase, F-TPase and V-ATPase. F-ATPase (ATP synthase) and V-ATP(prothn pump of endomembrance organelles such as lysosome and endosome) are closely similar in subunit structure and mechanism. They couples proton transport and ATPase chemistry through subunit rotation. Our extensive research results are showing:(1) Purified and membrane-bound F-ATPases are rotating during ATP hydrolysis. Their rotations are stochastic, and driven by hinge domain of the β subunit. (2) V-ATPases are also rotating proton pump, and their diverse isoforms specific for unique cells were found. (3) V-ATPase has domains required for specific localization and possibly for sensing organeller luminal pH. These results have been widely recognized in the field biochemistry and cell biology.
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