Oxidants induce Escherichia coli MarR glutathionylation in the presence of glutathione.

ABSTRACT: The results of protein thiols reacting with oxidants may be different in the presence or absence of glutathione (GSH). Upon exposure to oxidants, such as Cu²⁺ and polysulfide, the multiple drug resistant regulator MarR dimer in Escherichia coli is believed to form tetramers linked by disulfide bonds between its Cys⁸⁰ thiols. We confirmed this observation in the absence of GSH; however, the MarR-Cys⁸⁰ thiol was primarily glutathionylated in the presence of GSH after MarR was treated with various oxidants, including octasulfur (S₈), Cu²⁺, H₂O₂, ClO^-, and a NO donor. When using S₈ as the oxidizing agent, we identified four pathways to induce MarR-Cys⁸⁰ glutathionylation. Since E. coli

SUBMITTER: Wang T 

PROVIDER: S-EPMC12017873 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature