SecDF function and roles of the proton motive force in protein translocation
| Project/Area Number |
22370070
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | Kyoto University |
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Principal Investigator |
MORI Hiroyuki 京都大学, ウイルス研究所, 准教授 (10243271)
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| Co-Investigator(Kenkyū-buntansha) |
AKIYAMA Yoshinori 京都大学, ウイルス研究所, 教授 (10192460)
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| Co-Investigator(Renkei-kenkyūsha) |
TSUKAZAKI Tomoya 東京大学, 理学系研究科, 助教 (80436716)
MINAMINO Tohru 大阪大学, 生命機能研究科, 准教授 (20402993)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥18,850,000 (Direct Cost: ¥14,500,000、Indirect Cost: ¥4,350,000)
Fiscal Year 2012: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2011: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2010: ¥7,670,000 (Direct Cost: ¥5,900,000、Indirect Cost: ¥1,770,000)
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| Keywords | 生体膜 / SecDF / 膜透過 / in vivo光架橋実験 / イオントランスポーター / SecYEG / 細菌 / プロトン駆動力 / SecA / タンパク質膜透過 / SecA ATPase / 結晶構造解析 / カチオントランスポーター |
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| Research Abstract |
In bacteria, protein translocation across the membrane is stimulated by membrane-integrated components, SecDF. However, itsmolecular mechanisms remainunknown. In this study, we determined the crystal structure of Thermus thermophilusSecDF at 3.3 A resolutionand carried out a number of biochemical analysis based on the structural information.Finally, we propose a working hypothesis that SecDF functions as a membrane-integrated motor, powered by PMF, to achieveATP-independent full protein translocation ability of the Sec machinery
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Report
(4 results)
Research Products
(21 results)
