Does DsbA have chaperone-like activity?
DsbA showed chaperone-like activity similar to but weaker than that of protein disulfide isomerase in increasing reactivation and decreasing aggregation during the refolding of guanidine hydrochloride-denatured D-glyceraldehyde-3-phosphate dehydrogenase and rhodanese. The fact that both enzymes are devoid of disulfide bonds indicates the independence of the chaperone-like activity of DsbA from its thiol-protein oxidoreductase activity. The increased reactivation of D-glyceraldehyde-3-phosphate dehydrogenase by DsbA can be suppressed with increasing concentrations of a peptide of 21 amino acid residues, suggesting that the peptide binding ability of DsbA is responsible for its chaperone-like activity.
Zheng
W D
WD
Shanghai Research Center of Biotechnology, Academia Sinica, China.
Quan
H
H
Song
J L
JL
Yang
S L
SL
Wang
C C
CC
D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D007328:Insulin / Q000494:pharmacology; D007535:Isomerases / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D011485:Protein Binding; D011489:Protein Denaturation; D019704:Protein Disulfide-Isomerases; D017510:Protein Folding; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry* / Q000378:metabolism
D007328:Insulin; D018832:Molecular Chaperones; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D013884:Thiosulfate Sulfurtransferase; D007535:Isomerases; D019704:Protein Disulfide-Isomerases