2012 Fiscal Year Final Research Report
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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| Keywords | 生体膜 |
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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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[Journal Article] Structure and functionof a membrane component SecDF that enhances protein export.2011
Author(s)
Tsukazaki, T.*, Mori, H.*, Echizen, Y., Ishitani, R., Fukai, S., Tanaka, T., Perederina, A., Vassylyev, D. G., Kohno, T.,Matsurana, A. D., Ito, K. &Nureki O
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Journal Title
Nature
Volume: 474
Pages: 235-238
DOI
Peer Reviewed
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[Journal Article] Post liberation cleavage of signal peptides is catalyzed by the S2P protease in bacteria.2011
Author(s)
Saito, A., Hizukuri, Y., Matsuo, E.-i., Chiba, S., Mori, H., Nishimura, O., Ito, K., and Akiyama, Y
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Journal Title
Proc. Natl. Acad. Sci. USA
Volume: 108
Pages: 13740-13745
DOI
Peer Reviewed
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