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Molecular code for transmembrane-helix recognition by the Sec61 translocon

Author

Listed:
  • Tara Hessa

    (Center for Biomembrane Research, Stockholm University)

  • Nadja M. Meindl-Beinker

    (Center for Biomembrane Research, Stockholm University)

  • Andreas Bernsel

    (Stockholm Bioinformatics Center, AlbaNova, Stockholm University)

  • Hyun Kim

    (Center for Biomembrane Research, Stockholm University)

  • Yoko Sato

    (Center for Biomembrane Research, Stockholm University)

  • Mirjam Lerch-Bader

    (Center for Biomembrane Research, Stockholm University)

  • IngMarie Nilsson

    (Center for Biomembrane Research, Stockholm University)

  • Stephen H. White

    (University of California at Irvine, Irvine, California 92697-4560, USA)

  • Gunnar von Heijne

    (Center for Biomembrane Research, Stockholm University
    Stockholm Bioinformatics Center, AlbaNova, Stockholm University)

Abstract

Transmembrane α-helices in integral membrane proteins are recognized co-translationally and inserted into the membrane of the endoplasmic reticulum by the Sec61 translocon. A full quantitative description of this phenomenon, linking amino acid sequence to membrane insertion efficiency, is still lacking. Here, using in vitro translation of a model protein in the presence of dog pancreas rough microsomes to analyse a large number of systematically designed hydrophobic segments, we present a quantitative analysis of the position-dependent contribution of all 20 amino acids to membrane insertion efficiency, as well as of the effects of transmembrane segment length and flanking amino acids. The emerging picture of translocon-mediated transmembrane helix assembly is simple, with the critical sequence characteristics mirroring the physical properties of the lipid bilayer.

Suggested Citation

  • Tara Hessa & Nadja M. Meindl-Beinker & Andreas Bernsel & Hyun Kim & Yoko Sato & Mirjam Lerch-Bader & IngMarie Nilsson & Stephen H. White & Gunnar von Heijne, 2007. "Molecular code for transmembrane-helix recognition by the Sec61 translocon," Nature, Nature, vol. 450(7172), pages 1026-1030, December.
    • Handle: RePEc:nat:nature:v:450:y:2007:i:7172:d:10.1038_nature06387
    DOI: 10.1038/nature06387
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    Cited by:

    1. Zhaoxiang He & Mengchen Wu & Hongtao Tian & Liangdong Wang & Yiqi Hu & Fangzhu Han & Jiancang Zhou & Yong Wang & Long Zhou, 2024. "Euglena’s atypical respiratory chain adapts to the discoidal cristae and flexible metabolism," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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