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Structure of the native Sec61 protein-conducting channel. | LitMetric

Structure of the native Sec61 protein-conducting channel.

Nat Commun

Department of Molecular Structural Biology, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.

Published: September 2015

AI Article Synopsis

  • The study focuses on the Sec61 protein-conducting channel in mammalian cells, important for moving proteins into the endoplasmic reticulum (ER) membrane.
  • Researchers utilized cryo-electron tomography and ribosome profiling to examine native ribosome-Sec61 complexes on rough ER vesicles, finding the Sec61 channel in a laterally open conformation.
  • The findings challenge current models of protein translocation, indicating that the ribosome can facilitate the lateral opening of Sec61 independently of the presence of a nascent protein chain.

Article Abstract

In mammalian cells, secretory and membrane proteins are translocated across or inserted into the endoplasmic reticulum (ER) membrane by the universally conserved protein-conducting channel Sec61, which has been structurally studied in isolated, detergent-solubilized states. Here we structurally and functionally characterize native, non-solubilized ribosome-Sec61 complexes on rough ER vesicles using cryo-electron tomography and ribosome profiling. Surprisingly, the 9-Å resolution subtomogram average reveals Sec61 in a laterally open conformation, even though the channel is not in the process of inserting membrane proteins into the lipid bilayer. In contrast to recent mechanistic models for polypeptide translocation and insertion, our results indicate that the laterally open conformation of Sec61 is the only conformation present in the ribosome-bound translocon complex, independent of its functional state. Consistent with earlier functional studies, our structure suggests that the ribosome alone, even without a nascent chain, is sufficient for lateral opening of Sec61 in a lipid environment.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4598622PMC
http://dx.doi.org/10.1038/ncomms9403DOI Listing

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