Cited by 170Bacterial Genetics and BiotechnologyCellular transport and secretionRNA and protein synthesis mechanisms

The Sec translocon mediated protein transport in prokaryotes and eukaryotes.

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Denks, Kärt, Vogt, Andreas, Sachelaru, Ilie, Petriman, Narcis-Adrian, Kudva, Renuka, Koch, Hans-Georg·2014·Molecular Membrane Biology

Abstract

Protein transport via the Sec translocon represents an evolutionary conserved mechanism for delivering cytosolically-synthesized proteins to extra-cytosolic compartments. The Sec translocon has a three-subunit core, termed Sec61 in Eukaryotes and SecYEG in Bacteria. It is located in the endoplasmic reticulum of Eukaryotes and in the cytoplasmic membrane of Bacteria where it constitutes a channel that can be activated by multiple partner proteins. These partner proteins determine the mechanism of polypeptide movement across the channel. During SRP-dependent co-translational targeting, the ribosome threads the nascent protein directly into the Sec channel. This pathway is in Bacteria mainly dedicated for membrane proteins but in Eukaryotes also employed by secretory proteins. The alternative pathway, leading to post-translational translocation across the Sec translocon engages an ATP-dependent pushing mechanism by the motor protein SecA in Bacteria and a ratcheting mechanism by the lumenal chaperone BiP in Eukaryotes. Protein transport and biogenesis is also assisted by additional proteins at the lateral gate of SecY/Sec61α and in the lumen of the endoplasmic reticulum or in the periplasm of bacterial cells. The modular assembly enables the Sec complex to transport a vast array of substrates. In this review we summarize recent biochemical and structural information on the prokaryotic and eukaryotic Sec translocons and we describe the remarkably complex interaction network of the Sec complexes.

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Crossref · 10.3109/09687688.2014.907455

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  • The SecYEG translocon is universally conserved and mediates the translocation of newly synthesized proteins into and across the cytoplasmic membrane.

    “The universally conserved SecYEG translocon acts at the center of bacterial protein transport and mediates the translocation of newly synthesized proteins into and across the cytoplasmic membrane.”

    From The Dynamic SecYEG Translocon (2021) · cites this paper as Denks et al., 2014

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Authors
Denks, K., Vogt, A., Sachelaru, I., Petriman, N.-A., Kudva, R., & Koch, H.-G.
Affiliations
University of Freiburg (DE)
Corresponding author
Koch, Hans-Georg
Venue
Molecular Membrane Biology
Published
2014-03
Volume
31
Issue
2-3
Pages
58-84
ISSN
  • 0968-7688 (ISSN-L)
  • 1464-5203
OpenAlex
W1978110792
Cited by
170
References
431
Citations by year
2026: 4 · 2025: 7 · 2024: 18 · 2023: 10 · 2022: 16 · 2021: 18 · 2020: 17 · 2019: 15 · 2018: 7 · 2017: 22 · 2016: 9 · 2015: 21 · 2014: 6
FWCI
2.56
Type
journal article
Language
en
Open access
Locations
  • Molecular Membrane Biology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
Sec translocon, Sec61, SecYEG, protein translocation, SRP, post-translational translocation, SecA, BiP, endoplasmic reticulum, bacterial cytoplasmic membrane, membrane protein biogenesis, protein secretion, evolutionary conservation
MeSH terms
SEC Translocation Channels, Cell Membrane, Endoplasmic Reticulum, Membrane Proteins, Models, Molecular, Prokaryotic Cells, Signal Recognition Particle, Protein Transport, Eukaryota

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