Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33.

@article{Winter2005SevereOS,
  title={Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33.},
  author={Jeannette Winter and Katrin Linke and Anna Jatzek and Ursula Jakob},
  journal={Molecular cell},
  year={2005},
  volume={17 3},
  pages={381-92}
}
DnaK/DnaJ/GrpE constitutes the primary chaperone machinery in E. coli that functions to protect proteins against heat-induced protein aggregation. Surprisingly, upon exposure of cells to reactive oxygen species at elevated temperature, proteins are no longer protected by the DnaK system. Instead, they bind now to the redox-regulated chaperone Hsp33, which is activated by the same conditions that inactivate DnaK. The inactivation of DnaK seems to be induced by the dramatic decrease in… CONTINUE READING

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