Structure and function of a membrane component SecDF that enhances protein export

Tomoya Tsukazaki, Hiroyuki Mori, Yuka Echizen, Ryuichiro Ishitani, Shuya Fukai, Takeshi Tanaka, Anna Perederina, Dmitry G. Vassylyev, Toshiyuki Kohno, Andrés D. Maturana, Koreaki Ito () and Osamu Nureki ()
Additional contact information
Tomoya Tsukazaki: Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan
Hiroyuki Mori: Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan
Yuka Echizen: Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan
Ryuichiro Ishitani: Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan
Shuya Fukai: Structural Biology Laboratory, Synchrotron Radiation Research Organization, The University of Tokyo, Tokyo 113-0032, Japan
Takeshi Tanaka: Mitsubishi Kagaku Institute of Life Sciences, Machida-shi, Tokyo 194-8511, Japan
Anna Perederina: Schools of Medicine and Dentistry, University of Alabama at Birmingham
Dmitry G. Vassylyev: Schools of Medicine and Dentistry, University of Alabama at Birmingham
Toshiyuki Kohno: Mitsubishi Kagaku Institute of Life Sciences, Machida-shi, Tokyo 194-8511, Japan
Andrés D. Maturana: Nagaoka University of Technology, Niigata 940-2188, Japan
Koreaki Ito: Kyoto Sangyo University, Kita-ku, Kyoto 603-8555, Japan
Osamu Nureki: Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan

Nature, 2011, vol. 474, issue 7350, 235-238

Abstract: Structure of protein-export enhancer SecDF Protein translocation across the bacterial cell membrane is mediated by the SecYEG translocon and is enhanced by a membrane protein called SecDF, the function of which was unknown. In this study, Osamu Nureki and colleagues present a structural and functional analysis of SecDF. They show that it has 12 transmembrane domains and two major periplasmic domains (P1 and P4), and propose that SecDF functions as a membrane-integrated chaperone, powered by the proton motive force to perform protein translocation.

Date: 2011
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DOI: 10.1038/nature09980

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