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- Tsukazaki Tomoya
- Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo
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- Nureki Osamu
- Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo
抄録
Protein transport across membranes is a fundamental and essential cellular activity in all organisms. In bacteria, protein export across the cytoplasmic membrane, driven by dynamic interplays between the protein-conducting SecYEG channel (Sec translocon) and the SecA ATPase, is enhanced by the proton motive force (PMF) and a membrane-integrated Sec component, SecDF. However, the structure and function of SecDF have remained unclear. We solved the first crystal structure of SecDF, consisting of a pseudo-symmetrical 12-helix transmembrane domain and two protruding periplasmic domains. Based on the structural features, we proposed that SecDF functions as a membrane-integrated chaperone, which drives protein movement without using the major energetic currency, ATP, but with remarkable cycles of conformational changes, powered by the proton gradient across the membrane. By a series of biochemical and biophysical approaches, several functionally important residues in the transmembrane region have been identified and our model of the SecDF function has been verified.<br>
収録刊行物
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- BIOPHYSICS
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BIOPHYSICS 7 129-133, 2011
日本生物物理学会
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詳細情報 詳細情報について
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- CRID
- 1390001205223895552
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- NII論文ID
- 130001253088
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- ISSN
- 13492942
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可