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. 1995 Jun;177(11):3277–3282. doi: 10.1128/jb.177.11.3277-3282.1995

Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning.

V J Khisty 1, L L Randall 1
PMCID: PMC177021  PMID: 7768828

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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Selected References

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