A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB.
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.
Hardy
S J
SJ
Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.
Randall
L L
LL
D018528:ATP-Binding Cassette Transporters; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000378:metabolism*; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D007700:Kinetics; D008024:Ligands; D008320:Maltose / Q000378:metabolism; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D011487:Protein Conformation
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D008024:Ligands; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; C057842:SecB protein, Bacteria; C461599:maltose transport system, E coli; D008320:Maltose