ArticlePloS one2008
A novel OxyR sensor and regulator of hydrogen peroxide stress with one cysteine residue in Deinococcus radiodurans.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 113 citations in OpenAlex.
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- The DR2416/DR2415 two-component system is responsible for the radioresistance of Deinococcus radiodurans.Antonie van Leeuwenhoek · 2025Article
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- Atypical Bacilliredoxin AbxC Plays a Role in Responding to Oxidative Stress in Radiation-Resistant BacteriumAntioxidants (Basel, Switzerland) · 2021Article
- HP1021 is a redox switch protein identified in Helicobacter pylori.Nucleic acids research · 2021Article
- New insights into the activation of Radiation Desiccation Response regulon inJournal of biosciences · 2021Article
- Oxidative Stress in Bacteria and the Central Dogma of Molecular Biology.Frontiers in molecular biosciences · 2021Review
- How Microbes Defend Themselves From Incoming Hydrogen Peroxide.Frontiers in immunology · 2021Review
- The Novel ncRNA OsiR Positively Regulates Expression ofInternational journal of molecular sciences · 2020Article
- Protection from hydrogen peroxide stress relies mainly on AhpCF and KatA2 in Stenotrophomonas maltophilia.Journal of biomedical science · 2020Article
- PprI: The Key Protein in Response to DNA Damage inFrontiers in cell and developmental biology · 2020Review
- Structure and DNA damage-dependent derepression mechanism for the XRE family member DG-DdrO.Nucleic acids research · 2019Article
- Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species.FEMS microbiology reviews · 2019Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In bacteria, OxyR is a peroxide sensor and transcription regulator, which can sense the presence of reactive oxygen species and induce antioxidant system. When the cells are exposed to H(2)O(2), OxyR protein is activated via the formation of a disulfide bond between the two conserved cysteine residues (C199 and C208). In Deinococcus radiodurans, a previously unreported special characteristic of DrOxyR (DR0615) is found with only one conserved cysteine. dr0615 gene mutant is hypersensitive to H(2)O(2), but only a little to ionizing radiation. Site-directed mutagenesis and subsequent in vivo functional analyses revealed that the conserved cysteine (C210) is necessary for sensing H(2)O(2), but its mutation did not alter the binding characteristics of OxyR on DNA. Under oxidant stress, DrOxyR is oxidized to sulfenic acid form, which can be reduced by reducing reagents. In addition, quantitative real-time PCR and global transcription profile results showed that OxyR is not only a transcriptional activator (e.g., katE, drb0125), but also a transcriptional repressor (e.g., dps, mntH). Because OxyR regulates Mn and Fe ion transporter genes, Mn/Fe ion ratio is changed in dr0615 mutant, suggesting that the genes involved in Mn/Fe ion homeostasis, and the genes involved in antioxidant mechanism are highly cooperative under extremely oxidant stress. In conclusion, these findings expand the OxyR family, which could be divided into two classes: typical 2-Cys OxyR and 1-Cys OxyR.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.