DsbG, a protein disulfide isomerase with chaperone activity.
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.
Shao
F
F
Department of Biology, Program in Biomedical Sciences, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
Bader
M W
MW
Jakob
U
U
Bardwell
J C
JC
D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism; D004789:Enzyme Activation; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones / Q000032:analysis / Q000378:metabolism*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000032:analysis / Q000378:metabolism*; D033903:Periplasmic Proteins; D019704:Protein Disulfide-Isomerases / Q000032:analysis / Q000378:metabolism
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D033903:Periplasmic Proteins; D010088:Oxidoreductases; C109831:DsbG protein, E coli; D019704:Protein Disulfide-Isomerases