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Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes

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  • Tom A. Rapoport

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

Abstract

A decisive step in the biosynthesis of many proteins is their partial or complete translocation across the eukaryotic endoplasmic reticulum membrane or the prokaryotic plasma membrane. Most of these proteins are translocated through a protein-conducting channel that is formed by a conserved, heterotrimeric membrane-protein complex, the Sec61 or SecY complex. Depending on channel binding partners, polypeptides are moved by different mechanisms: the polypeptide chain is transferred directly into the channel by the translating ribosome, a ratcheting mechanism is used by the endoplasmic reticulum chaperone BiP, and a pushing mechanism is used by the bacterial ATPase SecA. Structural, genetic and biochemical data show how the channel opens across the membrane, releases hydrophobic segments of membrane proteins laterally into lipid, and maintains the membrane barrier for small molecules.

Suggested Citation

  • Tom A. Rapoport, 2007. "Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes," Nature, Nature, vol. 450(7170), pages 663-669, November.
    • Handle: RePEc:nat:nature:v:450:y:2007:i:7170:d:10.1038_nature06384
    DOI: 10.1038/nature06384
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    Cited by:

    1. Zhenrui Zhao & Mei Tian & Peng Zeng & Michael J. Christensen & Mingzhu Kou & Zhibiao Nan & Xingxu Zhang, 2022. "Modification of Cuticular Wax Composition and Biosynthesis by Epichloë gansuensis in Achnatherum inebrians at Different Growing Periods," Agriculture, MDPI, vol. 12(8), pages 1-12, August.
    2. Mohamed Mahameed & Pengli Wang & Shuai Xue & Martin Fussenegger, 2022. "Engineering receptors in the secretory pathway for orthogonal signalling control," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. Alex Dajkovic & Elizabeth Hinde & Calum MacKichan & Rut Carballido-Lopez, 2016. "Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane," PLOS ONE, Public Library of Science, vol. 11(6), pages 1-17, June.

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