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Thioredoxins are small, universal, disulfide isomerase proteins with required functions in oxidative stress response and RNA synthesis, among others. However, little is known about how anaerobic organisms maintain their intracellular redox balance or how thioredoxins may function differently under anaerobic metabolism. In this study, we investigated the roles of thioredoxins in sulfate-reducing microorganisms (SRMs). SRMs use sulfate as their primary electron acceptor in respiration to produce sulfide and are found in various environments including marine, freshwater sediments, guts and biofilms on ferrous metals where corrosion occurs. We found SRMs lack common redox maintenance molecules and macromolecules but have many and varied thioredoxins belonging to three types. Then, we probed their functions in the model SRM, Desulfovibrio vulgaris Hildenborough (DvH), by an in vivo disulfide bond capture proteomics experiment in both non-stressed and oxidatively stressed conditions. Our results demonstrated that thioredoxin 1 (Trx1) was essential in DvH and selectively responded to oxidative stress. Our data supported its role in RNA synthesis and energy transduction since Trx1 interacted with DsrC and QmoB. Thioredoxin 3 (Trx3), an atypical thioredoxin, was observed to have roles in sulfur transfer and dissimilatory sulfur metabolism. Next, DvH thioredoxin system protein encoding genes were deleted and single deletion mutant strains were tested for growth phenotypes under a variety of different electron donors, acceptors and toxic metal stresses. It is found that dissimilatory sulfate reduction improves resistance of DvH to metal stress. It appeared the sulfide provided certain protection to DvH from silver and uranium stress.
Majumder et al. (Fri,) studied this question.