Protein export through the bacterial Sec pathway
Abstract
The general secretory (Sec) pathway comprises an essential, ubiquitous and universal export machinery for most proteins that integrate into, or translocate through, the plasma membrane. Sec exportome polypeptides are synthesized as pre-proteins that have cleavable signal peptides fused to the exported mature domains. Recent advances have re-evaluated the interaction networks of pre-proteins with chaperones that are involved in pre-protein targeting from the ribosome to the SecYEG channel and have identified conformational signals as checkpoints for high-fidelity targeting and translocation. The recent structural and mechanistic insights into the channel and its ATPase motor SecA are important steps towards the elucidation of the allosteric crosstalk that mediates secretion. In this Review, we discuss recent biochemical, structural and mechanistic insights into the consecutive steps of the Sec pathway - sorting and targeting, translocation and release - in both co-translational and post-translational modes of export. The architecture and conformational dynamics of the SecYEG channel and its regulation by ribosomes, SecA and pre-proteins are highlighted. Moreover, we present conceptual models of the mechanisms and energetics of the Sec-pathway dependent secretion process in bacteria.
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E. coli exploits three main pathways for protein translocation to the periplasm: the SecB-dependent, the SRP-mediated and the twin-arginine transport pathways.
“Like other Gram-negative bacteria, E. coli exploits three main pathways for protein translocation to the periplasm: the SecB-dependent, the SRP-mediated and the twin-arginine transport (TAT) translocation pathways [131,132,133].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [133]
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- Authors
- Tsirigotaki, A., De Geyter, J., Šoštaric´, N., Economou, A., & Karamanou, S.
- Affiliations
- Rega Institute for Medical Research (BE)
- Corresponding author
- Economou, Anastassios
- Venue
- Nature Reviews Microbiology
- Published
- 2016-11-28
- Volume
- 15
- Issue
- 1
- Pages
- 21-36
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- OpenAlex
- W2559192784
- Cited by
- 447
- References
- 165
- Citations by year
- 2026: 54 · 2025: 41 · 2024: 44 · 2023: 40 · 2022: 40 · 2021: 54 · 2020: 37 · 2019: 63 · 2018: 48 · 2017: 26
- FWCI
- 6.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Lirias (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- Sec pathway, general secretory pathway, SecYEG channel, SecA ATPase, protein secretion, signal peptide, molecular chaperones, allosteric regulation
- MeSH terms
- SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Bacterial Proteins, Cell Membrane, Escherichia coli, Protein Conformation, Signal Transduction, Protein Transport, Protein Sorting Signals, Escherichia coli Proteins
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