A Kinetic Partitioning Model of Selective Binding of Nonnative Proteins by the Bacterial Chaperone SecB
- 25 January 1991
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 251 (4992) , 439-443
- https://doi.org/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.Keywords
This publication has 48 references indexed in Scilit:
- Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysisNature, 1989
- SecB functions as a cytosolic signal recognition factor for protein export in E. coliCell, 1989
- Secretion and membrane assemblyTrends in Biochemical Sciences, 1989
- Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteinsCell, 1989
- ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particleCell, 1988
- A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptidesNature, 1988
- 70K heat shock related proteins stimulate protein translocation into microsomesNature, 1988
- Characterization of an early intermediate in the folding of the .alpha. subunit of tryptophan synthase by hydrogen exchange measurementBiochemistry, 1985
- Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregationBiochemistry, 1979
- A quantitative treatment of the kinetics of the folding transition of ribonuclease ABiochemistry, 1976