Reports

A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB

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Science  25 Jan 1991:
Vol. 251, Issue 4992, pp. 439-443
DOI: 10.1126/science.1989077

Abstract

An in vitro assay for the interaction of SecB, a molecular chaperone from Escherichia coli, with polypeptide ligands was established based on the ability of SecB to block the refolding of denatured maltose-binding protein. Competition experiments show that SecB binds selectively to nonnative proteins with high affinity and without specificity for a particular sequence of amino acids. It is proposed that selectivity in binding is due to a kinetic partitioning of polypeptides between folding and association with SecB.