PMID:10788443

Citation	Shao, F, Bader, MW, Jakob, U and Bardwell, JC (2000) DsbG, a protein disulfide isomerase with chaperone activity. J. Biol. Chem. 275:13349-52
Abstract	DsbG, a protein disulfide isomerase present in the periplasm of Escherichia coli, is shown to function as a molecular chaperone. Stoichiometric amounts of DsbG are sufficient to prevent the thermal aggregation of two classical chaperone substrate proteins, citrate synthase and luciferase. DsbG was also shown to interact with refolding intermediates of chemically denatured citrate synthase and prevents their aggregation in vitro. Citrate synthase reactivation experiments in the presence of DsbG suggest that DsbG binds with high affinity to early unstructured protein folding intermediates. DsbG is one of the first periplasmic proteins shown to have general chaperone activity. This ability to chaperone protein folding is likely to increase the effectiveness of DsbG as a protein disulfide isomerase.
Links	PubMed
Keywords	Bacterial Proteins/analysis; Bacterial Proteins/metabolism; Enzyme Activation; Escherichia coli; Escherichia coli Proteins; Molecular Chaperones/analysis; Molecular Chaperones/metabolism; Oxidation-Reduction; Oxidoreductases/analysis; Oxidoreductases/metabolism; Periplasmic Proteins; Protein Disulfide-Isomerases/analysis; Protein Disulfide-Isomerases/metabolism
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