Journal
PROTEIN SCIENCE
Volume 19, Issue 6, Pages 1173-1179Publisher
WILEY-BLACKWELL
DOI: 10.1002/pro.392
Keywords
chaperone; SecA; SecB; protein export; protein-protein interaction; titration calorimetry; analytical sedimentation velocity centrifugation
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Funding
- NIH Research [GM29798]
- Hugo Wurdack Trust (University of Missouri)
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Protein export mediated by the general secretory Sec system in Escherichia coli proceeds by a dynamic transfer of a precursor polypeptide from the chaperone SecB to the SecA ATPase motor of the translocon and subsequently into and through the channel of the membrane-embedded SecYEG heterotrimer. The complex between SecA and SecB is stabilized by several separate sites of contact. Here we have demonstrated directly an interaction between the N-terminal residues 2 through 11 of SecA and the C-terminal 13 residues of SecB by isothermal titration calorimetry and analytical sedimentation velocity centrifugation. We discuss the unusual binding properties of SecA and SecB in context of a model for transfer of the precursor along the pathway of export.
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