ArticleJournal of bacteriology2009
Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed.
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.Protein science : a publication of the Protein Society · 2020Article
- Protein Translocation Activity in Surface-Supported Lipid Bilayers.Langmuir : the ACS journal of surfaces and colloids · 2019Article
- Direct visualization of theScience advances · 2019Article
- Coassembly of SecYEG and SecA Fully Restores the Properties of the Native Translocon.Journal of bacteriology · 2019Article
- Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis.Science advances · 2018Article
- SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels.FEMS microbiology letters · 2018Review
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- The basis of asymmetry in the SecA:SecB complex.Journal of molecular biology · 2015Article
- Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Mechanisms of Rose Bengal inhibition on SecA ATPase and ion channel activities.Biochemical and biophysical research communications · 2014Article
- Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels.Biochemical and biophysical research communications · 2013Article
- Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations.The Journal of biological chemistry · 2013Article
- The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Insights into the structure and assembly of Escherichia coli outer membrane protein A.The FEBS journal · 2012Review
- Characterization of the Escherichia coli SecA signal peptide-binding site.Journal of bacteriology · 2012Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Orientation of SecA and SecB in complex, derived from disulfide cross-linking.Journal of bacteriology · 2011Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
SecA is the ATPase that provides energy for translocation of precursor polypeptides through the SecYEG translocon in Escherichia coli during protein export. We showed previously that when SecA receives the precursor from SecB, the ternary complex is fully active only when two protomers of SecA are bound. Here we used variants of SecA and of SecB that populate complexes containing two protomers of SecA to different degrees to examine both the hydrolysis of ATP and the translocation of polypeptides. We conclude that the low activity of the complexes with only one protomer is the result of a low efficiency of coupling between ATP hydrolysis and translocation.
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Registered trials
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