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

Author

Listed:
  • 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
    Laboratory of Macromolecular Complexes, Center for Structural Biology of Challenging Proteins, 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)

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.

Suggested Citation

  • Tomoya Tsukazaki & Hiroyuki Mori & Yuka Echizen & Ryuichiro Ishitani & Shuya Fukai & Takeshi Tanaka & Anna Perederina & Dmitry G. Vassylyev & Toshiyuki Kohno & Andrés D. Maturana & Koreaki Ito & Osamu, 2011. "Structure and function of a membrane component SecDF that enhances protein export," Nature, Nature, vol. 474(7350), pages 235-238, June.
    • Handle: RePEc:nat:nature:v:474:y:2011:i:7350:d:10.1038_nature09980
    DOI: 10.1038/nature09980
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    Cited by:

    1. Keigo Fujiwara & Naoko Tsuji & Mayu Yoshida & Hiraku Takada & Shinobu Chiba, 2024. "Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Zikun Zhu & Shuai Wang & Shu-ou Shan, 2022. "Ribosome profiling reveals multiple roles of SecA in cotranslational protein export," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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