ArticleThe EMBO journal2002
The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Blue Native PAGE Analysis of Bacterial Secretion Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion.Scientific reports · 2020Article
- The Dynamic ATP-Driven Mechanism of Bacterial Protein Translocation and the Critical Role of Phospholipids.Frontiers in microbiology · 2019Review
- The Peptidisc, a simple method for stabilizing membrane proteins in detergent-free solution.eLife · 2018Article
- Alignment of the protein substrate hairpin along the SecA two-helix finger primes protein transport inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation.eLife · 2016Article
- Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linking.The Journal of biological chemistry · 2016Article
- Channel crossing: how are proteins shipped across the bacterial plasma membrane?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Molecular microbiology · 2015Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- TraK and TraB are conserved outer membrane proteins of the Neisseria gonorrhoeae Type IV secretion system and are expressed at low levels in wild-type cells.Journal of bacteriology · 2014Article
- Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Capturing the bacterial holo-complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations.The Journal of biological chemistry · 2013Article
- Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex.The Journal of cell biology · 2012Article
- Bacterial protein translocation requires only one copy of the SecY complex in vivo.The Journal of cell biology · 2012Article
- Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structure of the SecY complex unlocked by a preprotein mimic.Cell reports · 2012Article
- A single copy of SecYEG is sufficient for preprotein translocation.The EMBO journal · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli preprotein translocase comprises a membrane-embedded trimeric complex of SecY, SecE and SecG. Previous studies have shown that this complex forms ring-like assemblies, which are thought to represent the preprotein translocation channel across the membrane. We have analyzed the functional state and the quaternary structure of the SecYEG translocase by employing cross-linking and blue native gel electrophoresis. The results show that the SecYEG monomer is a highly dynamic structure, spontaneously and reversibly associating into dimers. SecG-dependent tetramers and higher order SecYEG multimers can also exist in the membrane, but these structures form at high SecYEG concentration or upon overproduction of the complex only. The translocation process does not affect the oligomeric state of the translocase and arrested preproteins can be trapped with SecYEG or SecYE dimers. Dissociation of the dimer into a monomer by detergent induces release of the trapped preprotein. These results provide direct evidence that preproteins cross the bacterial membrane, associated with a translocation channel formed by a dimer of SecYEG.
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