A structural model of the active ribosome-bound membrane protein insertase YidC
- Ludwig-Maximilians-Universität München, Germany
- University of Illinois at Urbana-Champaign, United States
- University of Illinois at Urbana-Champagin, United States
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.
Article and author information
Author details
Reviewing Editor
- Ramanujan S Hegde, MRC Laboratory of Molecular Biology, United Kingdom
Version history
- Received: April 8, 2014
- Accepted: July 8, 2014
- Accepted Manuscript published: July 10, 2014 (version 1)
- Version of Record published: August 7, 2014 (version 2)
Copyright
© 2014, Wickles et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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A structural model of the active ribosome-bound membrane protein insertase YidC
eLife 3:e03035.
https://doi.org/10.7554/eLife.03035
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