ArticleThe EMBO journal2003
Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Capture of endogenous lipids in peptidiscs and effect on protein stability and activity.iScience · 2024Article
- Article
- The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.Biochimica et biophysica acta. Biomembranes · 2020Article
- Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion.Scientific reports · 2020Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Investigating the stability of the SecA-SecYEG complex during protein translocation across the bacterial membrane.The Journal of biological chemistry · 2019Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- An alternate mode of oligomerization for E. coli SecA.Scientific reports · 2017Article
- 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
- 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
- Characterization of the minimal length of functional SecA in Escherichia coli.Biochemical and biophysical research communications · 2015Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Dynamic interaction of the sec translocon with the chaperone PpiD.The Journal of biological chemistry · 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
- Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation.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
- Defining the Escherichia coli SecA dimer interface residues through in vivo site-specific photo-cross-linking.Journal of bacteriology · 2013Article
- Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer.Biochemistry · 2013Article
- SecYEG activates GTPases to drive the completion of cotranslational protein targeting.The Journal of cell biology · 2013Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial preprotein translocase is comprised of a membrane-embedded oligomeric SecYEG structure and a cytosolic dimeric SecA ATPase. The associations within SecYEG oligomers and SecA dimers, as well as between these two domains are dynamic and reversible. Here, it is shown that a covalently linked SecYEG dimer forms a functional translocase and a high affinity binding site for monomeric and dimeric SecA in solution. The interaction between these two domains stimulates the SecA ATPase, and nucleotides modulate the affinity and ratio of SecA monomers and dimers bound to the linked SecYEG complex. During the translocation reaction, the SecA monomer remains in stable association with a SecYEG protomer and the translocating preprotein. The nucleotides and translocation-dependent changes of SecA-SecYEG associations and the SecA dimeric state may reflect important facets of the preprotein translocation reaction.
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