We analyzed the amount and redox state of cytoplasmic, membrane and periplasmic proteins in Escherichia coli mutants deficient in thioredoxin, thioredoxin reductase, glutathione and DsbA, by observing the electrophoretic profile of bacterial extracts after in vivo labelling with monobromobimane. Our results show that these mutations affected not only the amount and the redox state of proteins localized in the same compartment as the deficient oxidoreductase, but also those of the proteins localized in other compartments. These results concord with the hypothesis that there is a link between the redox reactions that occur in the cytoplasm and the periplasm. © 2001 Éditions scientifiques et médicales Elsevier SAS.
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