Reduction of protein disulfide bonds in an oxidizing environment
- 20 January 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 401 (2-3) , 104-108
- https://doi.org/10.1016/s0014-5793(96)01447-0
Abstract
Following retrograde transport to the endoplasmic reticulum (ER) the A‐subunit of cholera toxin (CTX‐A) is partially cleaved into CTX‐A1 and CTX‐A2 by reduction of a disulfide bridge [Majoul et al. (1996) J. Cell Biol. 133, 777–789], although the redox state in the ER favors disulfide formation. We show here that the disulfide bridge of CTX‐A is cleaved in vitro already at GSH/GSSG ratios between 1 and 3. Protein disulfide isomerase (PDI) exerts only a minor accelerating effect. Various mixed disulfide intermediates (CTX‐A1‐S‐S‐CTX‐A1; PDI‐S‐S‐A2; PDI‐S‐S‐A1) appear during CTX‐A reduction. These results indicate that in the ER protein disulfide formation and protein disulfide reduction can take place simultaneously.Keywords
This publication has 11 references indexed in Scilit:
- Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: studies with cholera toxin in Vero cells.The Journal of cell biology, 1996
- Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase.Journal of Biological Chemistry, 1994
- CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activityEuropean Journal of Biochemistry, 1993
- Oxidized Redox State of Glutathione in the Endoplasmic ReticulumScience, 1992
- A new multiphasic buffer system for sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of proteins and peptides with molecular masses 100 000–1000, and their detection with picomolar sensitivityElectrophoresis, 1991
- Control of Protein Exit from the Endoplasmic ReticulumAnnual Review of Cell Biology, 1989
- A C-terminal signal prevents secretion of luminal ER proteinsPublished by Elsevier ,1987
- Zur Reaktion von Cyclopropenonen mit Azomethinen, VIII Diphenylcyclopropenon und cyclische ImineSynthesis, 1986
- Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.Journal of Biological Chemistry, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970