Conformational transition of Sec machinery inferred from bacterial SecYE structures

Tomoya Tsukazaki, Hiroyuki Mori, Shuya Fukai, Ryuichiro Ishitani, Takaharu Mori, Naoshi Dohmae, Anna Perederina, Yuji Sugita, Dmitry G. Vassylyev, Koreaki Ito () and Osamu Nureki ()
Additional contact information
Tomoya Tsukazaki: Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan
Hiroyuki Mori: Institute for Virus Research, Kyoto University
Shuya Fukai: Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan
Ryuichiro Ishitani: The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan
Takaharu Mori: Advanced Science Institute,
Naoshi Dohmae: Biomolecular Characterization Team and CREST/JST, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
Anna Perederina: University of Alabama at Birmingham, Schools of Medicine and Dentistry, 402B Kaul Genetics Building, 720 20th Street South, Birmingham, Alabama 35294, USA
Yuji Sugita: Advanced Science Institute,
Dmitry G. Vassylyev: University of Alabama at Birmingham, Schools of Medicine and Dentistry, 402B Kaul Genetics Building, 720 20th Street South, Birmingham, Alabama 35294, USA
Koreaki Ito: Institute for Virus Research, Kyoto University
Osamu Nureki: Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan

Nature, 2008, vol. 455, issue 7215, 988-991

Abstract: Channel hopping: protein translocation through the SecA–SecY complex Newly synthesized proteins are translocated across the eukaryotic endoplasmic reticulum membrane or the prokaryotic plasma membrane through an evolutionarily conserved protein conducting channel or translocon known as Sec61 in eukaryotes and SecY in prokaryotes. In bacteria, the SecA ATPase is thought to be the motor for translocation through the SecY channel. Two papers by Tom Rapoport and colleagues report the long-awaited structure of the SecA–SecY complex from bacteria. The structure, reveals major conformational changes between both partners and suggests that SecA uses a two-helix finger to push translocating proteins into SecY's cytoplasmic funnel. Crosslinking studies provide further experimental support for this mechanism. In a third paper, Osamu Nureki and colleagues present a crystal structure of SecY bound to an anti-SecY Fab fragment revealing a pre-open state of the channel. Together these three papers provide novel insights into the path taken by a translocating protein. In News and Views, Anastassios Economou takes stock of where this work leaves current knowledge of this 'astonishing cellular nanomachine'.

Date: 2008
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DOI: 10.1038/nature07421

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