PMID:10025400
| Citation |
Jakob, U, Muse, W, Eser, M and Bardwell, JC (1999) Chaperone activity with a redox switch. Cell 96:341-52 |
|---|---|
| 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. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/metabolism; Bacterial Proteins/physiology; Cytoplasm/metabolism; Cytoplasm/microbiology; Disulfides/metabolism; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Heat-Shock Proteins/metabolism; Heat-Shock Proteins/physiology; Hot Temperature; Hydrogen Peroxide/pharmacology; Molecular Chaperones/metabolism; Molecular Chaperones/physiology; Molecular Sequence Data; Oxidation-Reduction/drug effects; Oxidative Stress/drug effects; Protein Folding; Reducing Agents/pharmacology |
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