MoaE Is Involved in Response to Oxidative Stress in Deinococcus radiodurans

Molybdenum ions are covalently bound to molybdenum pterin (MPT) to produce molybdenum cofactor (Moco), a compound essential for the catalytic activity of molybdenum enzymes, which is involved in a variety of biological functions. MoaE is the large subunit of MPT synthase and plays a key role in Moco synthesis. Here, we investigated the function of MoaE in Deinococcus radiodurans (DrMoaE) in vitro and in vivo, demonstrating that the protein contributed to the extreme resistance of D. radiodurans. The crystal structure of DrMoaE was determined by 1.9 angstrom resolution. DrMoaE was shown to be a dimer and the dimerization disappeared after Arg110 had been mutated. The deletion of drmoaE resulted in sensitivity to DNA damage stress and a slower growth rate in D. radiodurans. The increase in drmoaE transcript levels the and accumulation of intracellular reactive oxygen species levels under oxidative stress suggested that it was involved in the antioxidant process in D. radiodurans. In addition, treatment with the base analog 6-hydroxyaminopurine decreased survival and increased intracellular mutation rates in drmoaE deletion mutant strains. Our results reveal that MoaE plays a role in response to external stress mainly through oxidative stress resistance mechanisms in D. radiodurans.

Automated summary

In this study, the essential role of MoaE protein in the extreme resistance of Deinococcus radiodurans was demonstrated through in vitro and in vivo experiments. The crystal structure of DrMoaE was determined to be a dimer, which disappeared after mutation. Deletion of drmoaE gene resulted in sensitivity to DNA damage stress and slower growth rate in D. radiodurans. Increased transcript levels of drmoaE and accumulation of intracellular reactive oxygen species under oxidative stress suggested its involvement in antioxidant process.