Article
S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal α-helical lid.
The Journal of biological chemistry - 12 Jun 2020
Yang Jie, Zhang Hong, Gong Weibin, Liu Zhenyan, Wu Huiwen, Hu Wanhui, Chen Xinxin, Wang Lei, Wu Si, Chen Chang, Perrett Sarah
Abstract excerpt
Heat shock protein 70 (Hsp70) proteins are a family of ancient and conserved chaperones. Cysteine modifications have been widely detected among different Hsp70 family members in vivo, but their effects on Hsp70 structure and function are unclear. Here, we treated HeLa cells with diamide, which typically induces disulfide bond formation except in the presence of excess GSH, when glutathionylated cysteines...
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