Chaperone activity with a redox switch.
Article Details
- CitationCopy to clipboard
Jakob U, Muse W, Eser M, Bardwell JC
Chaperone activity with a redox switch.
Cell. 1999 Feb 5;96(3):341-52.
- PubMed ID
- 10025400 [ View in PubMed]
- Abstract
Hsp33, a member of a newly discovered heat shock protein family, was found to be a very potent molecular chaperone. Hsp33 is distinguished from all other known molecular chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function. In vitro and in vivo experiments suggest that Hsp33 protects cells from oxidants, leading us to conclude that we have found a protein family that plays an important role in the bacterial defense system toward oxidative stress.