Article
Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone.
The Journal of biological chemistry - 9 Apr 2010
Cremers Claudia M, Reichmann Dana, Hausmann Jens, Ilbert Marianne, Jakob Ursula
Abstract excerpt
Hsp33, a molecular chaperone specifically activated by oxidative stress conditions that lead to protein unfolding, protects cells against oxidative protein aggregation. Stress sensing in Hsp33 occurs via its C-terminal redox switch domain, which consists of a zinc center that responds to the presence of oxidants and an adjacent metastable linker region, which responds to unfolding conditions. Here we show that...
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