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Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion

Author

Listed:
  • Marko Gogala

    (Gene Center and Center for integrated Protein Science Munich, Feodor-Lynen-Strasse 25, University of Munich, 81377 Munich, Germany)

  • Thomas Becker

    (Gene Center and Center for integrated Protein Science Munich, Feodor-Lynen-Strasse 25, University of Munich, 81377 Munich, Germany)

  • Birgitta Beatrix

    (Gene Center and Center for integrated Protein Science Munich, Feodor-Lynen-Strasse 25, University of Munich, 81377 Munich, Germany)

  • Jean-Paul Armache

    (Gene Center and Center for integrated Protein Science Munich, Feodor-Lynen-Strasse 25, University of Munich, 81377 Munich, Germany)

  • Clara Barrio-Garcia

    (Gene Center and Center for integrated Protein Science Munich, Feodor-Lynen-Strasse 25, University of Munich, 81377 Munich, Germany)

  • Otto Berninghausen

    (Gene Center and Center for integrated Protein Science Munich, Feodor-Lynen-Strasse 25, University of Munich, 81377 Munich, Germany)

  • Roland Beckmann

    (Gene Center and Center for integrated Protein Science Munich, Feodor-Lynen-Strasse 25, University of Munich, 81377 Munich, Germany)

Abstract

Nascent secretory and membrane proteins are targeted to the Sec61 protein-conducting channel for translocation across or insertion into the endoplasmic reticulum membrane; here cryo-electron microscopy structures of eukaryotic ribosome–channel complexes show how this channel opens vertically during translocation of a secretory protein into the lumen of the endoplasmic reticulum and how it opens laterally during insertion of a transmembrane domain into the lipid bilayer.

Suggested Citation

  • Marko Gogala & Thomas Becker & Birgitta Beatrix & Jean-Paul Armache & Clara Barrio-Garcia & Otto Berninghausen & Roland Beckmann, 2014. "Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion," Nature, Nature, vol. 506(7486), pages 107-110, February.
    • Handle: RePEc:nat:nature:v:506:y:2014:i:7486:d:10.1038_nature12950
    DOI: 10.1038/nature12950
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