Zinc-binding domainRNA chaperoneAnti-termination activityCold stressThe heat shock protein 33 (Hsp33), a redox-regulated molecular chaperone, protectsEscherichia colifrom H2O2and heat-induced stress. Although the function of oxidized Hsp33 has been studied extensively, the role of zinc-bound Hsp33 ...
The redox-regulated chaperone Hsp33 is specifically activated upon exposure of cells to peroxide stress at elevated temperatures. Here we show that Hsp33 harbors two interdependent stress-sensing regions located in the C-terminal redox-switch domain of Hsp33: a zinc center sensing peroxide stress ...
Heat shock protein 33 (Hsp33) is activated in the presence of H2O2 by a very interesting redox switch based on a tetra-coordinated zinc–cysteine complex present in the fully reduced and inactive protein form. The oxidation of this zinc center by H2O2 induces formation of two...
We report here a theoretical study of the step-by-step sequence of the overall process starting with the oxidation of the first cysteine residue and ending with the zinc release. Each reaction step is characterized by its Gibbs free energy barrier (∆G ‡). It is predicted that the ...
Two of the four conserved zinc-coordinating cysteines are in the end of the N-terminal domain, and the other two are in the cleaved C-terminal domain. The structural information and subsequent biochemical characterizations suggest that the redox switch of Hsp33 occurrs by a reversible ...
Dyson, The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold, J. Mol. Biol. 341 (2004) 893-899.Won HS, Low LY, Guzman RD, Martines-Yamout M, Jakob U, and Dyson HJ. The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold. J Mol ...