Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese.
Protein disulfide-isomerase (PDI) in near stoichiometric concentrations promotes reactivation and prevents aggregation of guanidine-hydrochloride-denatured rhodanese during refolding upon dilution. PDI also suppresses aggregation of rhodanese during thermal inactivation. The above-mentioned properties displayed by PDI completely satisfy the definition of chaperone and provide additional evidence to confirm the hypothesis proposed previously [Wang, C. C. & Tsou, C. L. (1993) FASEB J. 7, 1515-1517] that PDI is both an enzyme and a chaperone. Since rhodanese contains no disulfide bonds, the chaperone-like activity of PDI acting on rhodanese is independent of its disulfide-isomerase activity.
Song
J L
JL
National Laboratory of Macromolecules, Academia Sinica, Beijing, China.
Wang
C C
CC
D000818:Animals; D002417:Cattle; D004789:Enzyme Activation; D005453:Fluorescence; D007535:Isomerases / Q000378:metabolism / Q000494:pharmacology*; D007700:Kinetics; D018832:Molecular Chaperones / Q000494:pharmacology*; D011489:Protein Denaturation; D019704:Protein Disulfide-Isomerases; D017510:Protein Folding; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013696:Temperature; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry* / Q000378:metabolism; D014364:Tryptophan / Q000378:metabolism
D018832:Molecular Chaperones; D013438:Sulfhydryl Compounds; D014364:Tryptophan; D013884:Thiosulfate Sulfurtransferase; D007535:Isomerases; D019704:Protein Disulfide-Isomerases