Abstract
An early step in the export of maltose-binding protein to the periplasm is interaction with the molecular chaperone SecB. We demonstrate that binding to SecB in vivo is determined by a kinetic partitioning between the folding of maltose-binding protein to its native state and its association with SecB. A complex of SecB and a species of maltose-binding protein that folds slowly is shown to be longer-lived than a complex of the wild-type maltose-binding protein and SecB. In addition, we show that incomplete nascent chains, which are unable to fold, remain complexed with SecB.
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Dates
Type | When |
---|---|
Created | 8 years, 9 months ago (Nov. 14, 2016, 12:16 p.m.) |
Deposited | 4 years, 1 month ago (July 29, 2021, 1:49 p.m.) |
Indexed | 1 month, 3 weeks ago (July 11, 2025, 6:44 a.m.) |
Issued | 30 years, 3 months ago (June 1, 1995) |
Published | 30 years, 3 months ago (June 1, 1995) |
Published Print | 30 years, 3 months ago (June 1, 1995) |
@article{Khisty_1995, title={Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning}, volume={177}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.177.11.3277-3282.1995}, DOI={10.1128/jb.177.11.3277-3282.1995}, number={11}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Khisty, V J and Randall, L L}, year={1995}, month=jun, pages={3277–3282} }