Thiol Reductases in Deinococcus Bacteria and Roles in Stress Tolerance.

ABSTRACT: Deinococcus species possess remarkable tolerance to extreme environmental conditions that generate oxidative damage to macromolecules. Among enzymes fulfilling key functions in metabolism regulation and stress responses, thiol reductases (TRs) harbour catalytic cysteines modulating the redox status of Cys and Met in partner proteins. We present here a detailed description of Deinococcus TRs regarding gene occurrence, sequence features, and physiological functions that remain poorly characterised in this genus. Two NADPH-dependent thiol-based systems are present in Deinococcus. One involves thioredoxins, disulfide reductases providing electrons to protein partners involved notably in peroxide scavenging or in preserving protein redox status. The other is based on bacill

SUBMITTER: de Groot A 

PROVIDER: S-EPMC8945050 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature