ArticleProtein science : a publication of the Protein Society2004
Sites of interaction between SecA and the chaperone SecB, two proteins involved in export.
Article in Protein science : a publication of the Protein Society, 2004. 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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Who cites it
21 citing papers in PubMed, 44 citations in OpenAlex.
- Membrane association and polar localization of theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Complete Genome Sequences ofMicrobiology resource announcements · 2022Article
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.EMBO reports · 2020Article
- Article
- Structural insights into chaperone addiction of toxin-antitoxin systems.Nature communications · 2019Article
- Penetration into membrane of amino-terminal region of SecA when associated with SecYEG in active complexes.Protein science : a publication of the Protein Society · 2018Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Determination of the intracellular concentration of the export chaperone SecB in Escherichia coli.PloS one · 2017Article
- The basis of asymmetry in the SecA:SecB complex.Journal of molecular biology · 2015Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Article
- Multitasking SecB chaperones in bacteria.Frontiers in microbiology · 2014Review
- The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA.Protein science : a publication of the Protein Society · 2010Article
- Characterization of interactions between proteins using site-directed spin labeling and electron paramagnetic resonance spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2010Article
- Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA.Journal of bacteriology · 2009Article
- A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.Journal of molecular biology · 2007Article
- Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export.Protein science : a publication of the Protein Society · 2006Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
SecB, a small tetrameric cytosolic chaperone in Escherichia coli, facilitates the export of precursor poly-peptides by maintaining them in a nonnative conformation and passing them to SecA, which is a peripheral member of the membrane-bound translocation apparatus. It has been proposed by several laboratories that as SecA interacts with various components along the export pathway, it undergoes conformational changes that are crucial to its function. Here we report details of molecular interactions between SecA and SecB, which may serve as conformational switches. One site of interaction involves the final C-terminal 21 amino acids of SecA, which are positively charged and contain zinc. The C terminus of each subunit of the SecA dimer makes contact with the flat beta-sheet that is formed by each dimer of the SecB tetramer. Here we demonstrate that a second interaction exists between the extreme C-terminal alpha-helix of SecB and a site on SecA, as yet undefined but different from the C terminus of SecA. We investigated the energetics of the interactions by titration calorimetry and characterized the hydrodynamic properties of complexes stabilized by both interactions or each interaction singly using sedimentation velocity centrifugation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.