ArticlePloS one2012
The mycobacterial LysR-type regulator OxyS responds to oxidative stress and negatively regulates expression of the catalase-peroxidase gene.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
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- TrmB Family Transcription Factor as a Thiol-Based Regulator of Oxidative Stress Response.mBio · 2022Article
- Investigating a putative transcriptional regulatory protein encoded by Rv1719 gene of Mycobacterium tuberculosis.The protein journal · 2022Article
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- A novel stress-inducible CmtR-ESX3-ZnThe Journal of biological chemistry · 2020Article
- Multiple transcription factors co-regulate the Mycobacterium tuberculosis adaptation response to vitamin C.BMC genomics · 2019Article
- Reduce, Induce, Thrive: Bacterial Redox Sensing during Pathogenesis.Journal of bacteriology · 2018Review
- HpoR, a novel c-di-GMP effective transcription factor, links the second messenger's regulatory function to the mycobacterial antioxidant defense.Nucleic acids research · 2018Article
- Thiol-based redox switches in prokaryotes.Biological chemistry · 2015Review
- An altered Mycobacterium tuberculosis metabolome induced by katG mutations resulting in isoniazid resistance.Antimicrobial agents and chemotherapy · 2014Article
- Radiation-sensitive gene A (RadA) targets DisA, DNA integrity scanning protein A, to negatively affect cyclic Di-AMP synthesis activity in Mycobacterium smegmatis.The Journal of biological chemistry · 2013Article
- Positive feedback regulation of stgR expression for secondary metabolism in Streptomyces coelicolor.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protection against oxidative stress is one of the primary defense mechanisms contributing to the survival of Mycobacterium tuberculosis in the host. In this study, we provide evidence that OxyS, a LysR-type transcriptional regulator functions as an oxidative stress response regulator in mycobacteria. Overexpression of OxyS lowers expression of the catalase-peroxidase (KatG) gene in M. smegmatis. OxyS binds directly with the katG promoter region and a conserved, GC-rich T-N(11)-A motif for OxyS binding was successfully characterized in the core binding site. Interestingly, the DNA-binding activity of OxyS was inhibited by H(2)O(2), but not by dithiothreitol. Cys25, which is situated at the DNA-binding domain of OxyS, was found to have a regulatory role for the DNA-binding ability of OxyS in response to oxidative stress. In contrast, the other three cysteine residues in OxyS do not appear to have this function. Furthermore, the mycobacterial strain over-expressing OxyS had a higher sensitivity to H(2)O(2). Thus, OxyS responds to oxidative stress through a unique cysteine residue situated in its DNA-binding domain and negatively regulates expression of the katG gene. These findings uncover a specific regulatory mechanism for mycobacterial adaptation to oxidative stress.
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