Science. 1991 Jan 25;251(4992):439-43.

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

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Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.

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.

PMID:: 1989077; [PubMed - indexed for MEDLINE]

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Interaction of SecB with intermediates along the folding pathway of maltose-binding protein. [Protein Sci. 1995]
Interaction of SecB with intermediates along the folding pathway of maltose-binding protein.
Diamond DL, Strobel S, Chun SY, Randall LL. Protein Sci. 1995 Jun; 4(6):1118-23.
Kinetic partitioning. Poising SecB to favor association with a rapidly folding ligand. [J Biol Chem. 1997]
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Diamond DL, Randall LL. J Biol Chem. 1997 Nov 14; 272(46):28994-8.
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Review Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export. [Philos Trans R Soc Lond B Biol...]
Review Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export.
Hardy SJ, Randall LL. Philos Trans R Soc Lond B Biol Sci. 1993 Mar 29; 339(1289):343-52; discussion 352-4.
Review Tinkering with transporters: periplasmic binding protein-dependent maltose transport in E. coli. [J Bioenerg Biomembr. 1993]
Review Tinkering with transporters: periplasmic binding protein-dependent maltose transport in E. coli.
Shuman HA, Panagiotidis CH. J Bioenerg Biomembr. 1993 Dec; 25(6):613-20.

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Yen YT, Seepersaud R, Bensing BA, Sullam PM. J Bacteriol. 2011 Jul; 193(13):3165-74. Epub 2011 Apr 29.
The rate of folding dictates substrate secretion by the Escherichia coli hemolysin type 1 secretion system. [J Biol Chem. 2010]
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Bakkes PJ, Jenewein S, Smits SH, Holland IB, Schmitt L. J Biol Chem. 2010 Dec 24; 285(52):40573-80. Epub 2010 Oct 22.

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

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