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Protein Structure and Folding
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- Protein Structure and FoldingOpen Access
Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response
Journal of Biological ChemistryVol. 291Issue 13p6967–6981Published online: January 28, 2016- Hong Zhang
- Jie Yang
- Si Wu
- Weibin Gong
- Chang Chen
- Sarah Perrett
Cited in Scopus: 32DnaK is the major bacterial Hsp70, participating in DNA replication, protein folding, and the stress response. DnaK cooperates with the Hsp40 co-chaperone DnaJ and the nucleotide exchange factor GrpE. Under non-stress conditions, DnaK binds to the heat shock transcription factor σ32 and facilitates its degradation. Oxidative stress results in temporary inactivation of DnaK due to depletion of cellular ATP and thiol modifications such as glutathionylation until normal cellular ATP levels and a reducing environment are restored.