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The Sec translocon mediated protein transport in prokaryotes and eukaryotes.
Open accessAbstract
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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“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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Molecular Characterization of a Novel Mammalian DnaJ-Like Sec63p Homolog
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Two Cooperating Helices Constitute the Lipid-binding Domain of the Bacterial SRP Receptor
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Export of β-Lactamase Is Independent of the Signal Recognition Particle
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Self-citationThe Bacterial Translocon SecYEG Opens upon Ribosome Binding
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The Signal Sequence Influences Post-Translational ER Translocation at Distinct Stages
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Self-citationThe evolution of YidC/Oxa/Alb3 family in the three domains of life: a phylogenomic analysis
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Flagged first, then by citations
Research works printed but not linked: 4
- Castanié-Cornet M-P, 2013, Biochim Biophys Acta – Mol Cell Res
- Keller RCA, 2011, Cell Mol Biol Lett, 16, 40
- Nakashima K, 2012, J Bacteriol, 152, 27
- Tseng TT, 1999, J Mol MicroBio Biotechnol, 1, 107
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Metadata
- 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
- Publisher
- Informa UK Limited
- 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
- bronze
- doi.org
- 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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