ArticleProtein science : a publication of the Protein Society2006
Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- 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
- Article
- The SecB-like chaperone Rv1957 from Mycobacterium tuberculosis: crystallization and X-ray crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2016Article
- The basis of asymmetry in the SecA:SecB complex.Journal of molecular biology · 2015Article
- Article
- 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
- Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis.Applied and environmental microbiology · 2012Article
- Mapping of the SecA·SecY and SecA·SecG interfaces by site-directed in vivo photocross-linking.The Journal of biological chemistry · 2011Article
- 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
- The active ring-like structure of SecA revealed by electron crystallography: conformational change upon interaction with SecB.Journal of structural biology · 2007Article
- Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling.Journal of molecular biology · 2006Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The general secretory, Sec, system translocates precursor polypeptides from the cytosol across the cytoplasmic membrane in Escherichia coli. SecB, a small cytosolic chaperone, captures the precursor polypeptides before they fold and delivers them to the membrane translocon through interactions with SecA. Both SecB and SecA display twofold symmetry and yet the complex between the two is stabilized by contacts that are distributed asymmetrically. Two distinct regions of interaction have been defined previously and here we identify a third. Calorimetric studies of complexes stabilized by different subsets of these interactions were carried out to determine the binding affinities and the thermodynamic parameters that underlie them. We show here that there is no change in affinity when either one of two contact areas out of the three is lacking. This fact and the asymmetry of the binding contacts may be important to the function of the complex in protein export.
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