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Visualization of a polytopic membrane protein during SecY-mediated membrane insertion

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  • Lukas Bischoff

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

  • Stephan Wickles

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

  • Otto Berninghausen

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

  • Eli O. van der Sluis

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

  • Roland Beckmann

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

Abstract

The biogenesis of polytopic membrane proteins occurs co-translationally on ribosomes that are tightly bound to a membrane-embedded protein-conducting channel: the Sec-complex. The path that is followed by nascent proteins inside the ribosome and the Sec-complex is relatively well established; however, it is not clear what the fate of the N-terminal transmembrane domains (TMDs) of polytopic membrane proteins is when the C-terminal TMDs domains are not yet synthesized. Here, we present the sub-nanometer cryo-electron microscopy structure of an in vivo generated ribosome-SecY complex that carries a membrane insertion intermediate of proteorhodopsin (PR). The structure reveals a pre-opened Sec-complex and the first two TMDs of PR already outside the SecY complex directly in front of its proposed lateral gate. Thus, our structure is in agreement with positioning of N-terminal TMDs at the periphery of SecY, and in addition, it provides clues for the molecular mechanism underlying membrane protein topogenesis.

Suggested Citation

  • Lukas Bischoff & Stephan Wickles & Otto Berninghausen & Eli O. van der Sluis & Roland Beckmann, 2014. "Visualization of a polytopic membrane protein during SecY-mediated membrane insertion," Nature Communications, Nature, vol. 5(1), pages 1-8, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5103
    DOI: 10.1038/ncomms5103
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