MoaE Is Involved in Response to Oxidative Stress in <i>Deinococcus radiodurans</i>
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...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-01-01
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| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/24/3/2441 |
| Summary: | 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 <i>Deinococcus radiodurans</i> (DrMoaE) in vitro and in vivo, demonstrating that the protein contributed to the extreme resistance of <i>D. radiodurans</i>. The crystal structure of DrMoaE was determined by 1.9 Å resolution. DrMoaE was shown to be a dimer and the dimerization disappeared after Arg110 had been mutated. The deletion of <i>drmoaE</i> resulted in sensitivity to DNA damage stress and a slower growth rate in <i>D. radiodurans</i>. The increase in <i>drmoaE</i> transcript levels the and accumulation of intracellular reactive oxygen species levels under oxidative stress suggested that it was involved in the antioxidant process in <i>D. radiodurans</i>. In addition, treatment with the base analog 6-hydroxyaminopurine decreased survival and increased intracellular mutation rates in <i>drmoaE</i> deletion mutant strains. Our results reveal that MoaE plays a role in response to external stress mainly through oxidative stress resistance mechanisms in <i>D. radiodurans</i>. |
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| ISSN: | 1661-6596 1422-0067 |