A structural model of the active ribosome-bound membrane protein insertase YidC

Stephan Wickles, Abhishek Singharoy, Jessica Andreani, Stefan Seemayer, Lukas Bischoff, Otto Berninghausen, Johannes Soeding, Klaus Schulten, Eli O. van der Sluis, Roland Beckmann

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40 Scopus citations

Abstract

The integration of most membrane proteins into the cytoplasmic membrane of bacteria occurs co-translationally. The universally conserved YidC protein mediates this process either individually as a membrane protein insertase, or in concert with the SecY complex. Here, we present a structural model of YidC based on evolutionary co-variation analysis, lipid-versus-protein-exposure and molecular dynamics simulations. The model suggests a distinctive arrangement of the conserved five transmembrane domains and a helical hairpin between transmembrane segment 2 (TM2) and TM3 on the cytoplasmic membrane surface. The model was used for docking into a cryo-electron microscopy reconstruction of a translating YidC-ribosome complex carrying the YidC substrate FOc. This structure reveals how a single copy of YidC interacts with the ribosome at the ribosomal tunnel exit and identifies a site for membrane protein insertion at the YidC protein-lipid interface. Together, these data suggest a mechanism for the co-translational mode of YidC-mediated membrane protein insertion.

Original languageEnglish (US)
Article numbere03035
Pages (from-to)1-17
Number of pages17
JournaleLife
Volume3
Issue numberJuly2014
DOIs
StatePublished - Jul 10 2014

ASJC Scopus subject areas

  • Neuroscience(all)
  • Immunology and Microbiology(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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    Wickles, S., Singharoy, A., Andreani, J., Seemayer, S., Bischoff, L., Berninghausen, O., Soeding, J., Schulten, K., van der Sluis, E. O., & Beckmann, R. (2014). A structural model of the active ribosome-bound membrane protein insertase YidC. eLife, 3(July2014), 1-17. [e03035]. https://doi.org/10.7554/eLife.03035