Molecular mechanism of protein translocation stimulation by SecDF using proton motive force
Project/Area Number |
17K07334
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Functional biochemistry
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Research Institution | Kyoto University |
Principal Investigator |
Mori Hiroyuki 京都大学, ウイルス・再生医科学研究所, 准教授 (10243271)
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Project Period (FY) |
2017-04-01 – 2021-03-31
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Project Status |
Completed (Fiscal Year 2020)
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Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2019: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2018: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2017: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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Keywords | SecDF / プロトン駆動力 / タンパク質膜透過 / PMF / 細菌 / 分泌 / PpiD / in vivo光架橋実験 / 膜タンパク質 / エネルギー変換 |
Outline of Final Research Achievements |
The membrane protein complex SecDF promotes protein translocation in bacteria using proton-driven force, but the details of its molecular mechanism remain unclear. In this study, by identifying factors that are in close proximity to SecDF in living cells, we found that the periplasmic chaperone PpiD is involved in the protein translocation of a substrate by working together with SecDF. In addition, we determined high-resolution crystal structures of another conformational state of SecDF. These results provide important insights into the mechanism of SecDF-mediated stimulation of protein translocation.
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Academic Significance and Societal Importance of the Research Achievements |
タンパク質の膜透過反応は全ての生物に必須の現象であり、その分子機構の理解は細胞生物学の重要な研究課題の1つである。加えて、近年病原性細菌の多剤耐性化による院内感染の増加は大きな社会問題となっており、これまでとは作用機序の異なる薬の開発が待たれている。SecDFは細菌に特有の因子であるのに加え、大きな機能ドメインを細胞質外に持つことから、創薬の有用なターゲット候補として期待されている。効率良い創薬を進めるには、本研究による分子機構の理解は非常に意義が大きい。
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Report
(5 results)
Research Products
(28 results)
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[Journal Article] Tree of motility;A proposed history of motility systems in the tree of life2020
Author(s)
M Miyata, R C Robinson, T QP Uyeda, Y Fukumori, S Fukushima, S Haruta, M Homma, K Inaba, M Ito, C Kaito, K Kato, TKenri, Y Kinosita, S Kojima, T Minamino, H Mori, S Nakamura, D Nakane, K Nakayama, M Nishiyama, S Shibata, K Shimabukuro, M Tamakoshi, A Taoka, Y Tashiro, ITulum, HiWada, K Wakabayashi
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Journal Title
Genes to Cells
Volume: 25
Issue: 1
Pages: 6-21
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF2017
Author(s)
Arata Furukawa, Kunihito Yoshikaie, Takaharu Mori, Hiroyuki Mori, Yusuke V. Morimoto, Yasunori Sugano, Shigehiro Iwaki, Tohru Minamino, Yuji Sugita, Yoshiki Tanaka, Tomoya Tsukazaki
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Journal Title
Cell Reports
Volume: 19
Issue: 5
Pages: 1-7
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] BepA mediates productive transfer of substrate proteins to the β-barrel assembly machinery (BAM) complex.2017
Author(s)
Daimon, Y., Masui, C., Tanaka, Y., Shiota, T., Suzuki, T., Miyazaki, R., Sakurada, H., Lithgow, T., Dohmae, N., Mori, H., Tsukazaki, T., Narita, S. and Akiyama, Y.
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Journal Title
Mol. Microbiol.
Volume: 106
Issue: 5
Pages: 760-776
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Presentation] Protein translocation motor SecDF.2017
Author(s)
Tsukazaki, T., Furukawa, A., Yoshikaie, K., Mori, T., Mori, H., Morimoto, V. Y., Sugano, T., Iwaki, S., Minamino, T., Sugita, Y. and Tanaka, T
Organizer
日本生物物理学会第55回年会 シンポジウム「構造生命科学の新しい潮流」
Related Report
Invited
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