Hsp33 protein is a molecular chaperone, distinguished from all other known 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 disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.[1]
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Chaperones | Functions & Types
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References
- ^ Jakob U, Muse W, Eser M, Bardwell JC (1999). "Chaperone activity with a redox switch". Cell. 96 (3): 341–352. doi:10.1016/S0092-8674(00)80547-4. PMID 10025400.
This page was last edited on 13 June 2023, at 10:35