Structure of the native Sec61 protein-conducting channel

Stefan Pfeffer, Laura Burbaum, Pia Unverdorben, Markus Pech, Yuxiang Chen, Richard Zimmermann, Roland Beckmann and Friedrich Förster ()
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Stefan Pfeffer: Max-Planck Institute of Biochemistry, Am Klopferspitz 18
Laura Burbaum: Max-Planck Institute of Biochemistry, Am Klopferspitz 18
Pia Unverdorben: Max-Planck Institute of Biochemistry, Am Klopferspitz 18
Markus Pech: Gene Center and Center for integrated Protein Science Munich, University of Munich
Yuxiang Chen: Max-Planck Institute of Biochemistry, Am Klopferspitz 18
Richard Zimmermann: Saarland University
Roland Beckmann: Gene Center and Center for integrated Protein Science Munich, University of Munich
Friedrich Förster: Max-Planck Institute of Biochemistry, Am Klopferspitz 18

Nature Communications, 2015, vol. 6, issue 1, 1-7

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms9403

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