Polymerization of Oxidized DJ-1 via Noncovalent and Covalent Binding: Significance of Disulfide Bond Formation.

ABSTRACT: The reactive cysteine residue at position 106 (Cys106) of DJ-1 is preferentially oxidized under oxidative stress, generating oxidized DJ-1 (oxDJ-1). Oxidation of Cys106 to sulfinic acid changes the biologic action of DJ-1 and increases its cytoprotective properties. The similar activation step is known in peroxiredoxins (Prxs), in which oxidation of reactive Cys to sulfinic acid induces polymerization of Prxs and changes its enzyme characteristic from peroxidase to molecular chaperone. In the present study, oxDJ-1 was prepared and its polymerization and related amino acid residues were investigated. We found that oxDJ-1 formed a characteristic polymer with disulfide bonds and with noncovalent and covalent binding other than disulfide. The physiological concentration of glutathione resolved

SUBMITTER: Kobayashi M 

PROVIDER: S-EPMC6648325 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature