ArticlePloS one2012
Characterization of OxyR as a negative transcriptional regulator that represses catalase production in Corynebacterium diphtheriae.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- Elucidating the Mechanism of Temporal Adaptation to Hydrogen Peroxide-Induced Oxidative Stress in Corynebacterium glutamicum.Microbial biotechnology · 2025Article
- Transcription factor OxyR regulates sulfane sulfur removal and L-cysteine biosynthesis inApplied and environmental microbiology · 2023Article
- Effects of OxyR regulator on oxidative stress, Apx toxin secretion and virulence ofFrontiers in cellular and infection microbiology · 2023Article
- Insights of OxyR role in mechanisms of host-pathogen interaction of Corynebacterium diphtheriae.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022Article
- Mechanisms underlying interactions between two abundant oral commensal bacteria.The ISME journal · 2022Article
- Overview of the Cellular Stress Responses Involved in Fatty Acid Overproduction in E. coli.Molecular biotechnology · 2022Review
- Article
- Successive mycelial subculturing decreased lignocellulase activity and increased ROS accumulation inFrontiers in microbiology · 2022Article
- OsnR is an autoregulatory negative transcription factor controlling redox-dependent stress responses in Corynebacterium glutamicum.Microbial cell factories · 2021Article
- Insertional Inactivation ofMicroorganisms · 2021Article
- How Microbes Defend Themselves From Incoming Hydrogen Peroxide.Frontiers in immunology · 2021Review
- Distinct HFrontiers in microbiology · 2021Article
- Mycoredoxins Are Required for Redox Homeostasis and Intracellular Survival in the Actinobacterial PathogenAntioxidants (Basel, Switzerland) · 2019Article
- The osnR gene of Corynebacterium glutamicum plays a negative regulatory role in oxidative stress responses.Journal of industrial microbiology & biotechnology · 2019Article
- Molecular Mechanisms of AhpC in Resistance to Oxidative Stress inFrontiers in microbiology · 2019Article
- Structural snapshots of OxyR reveal the peroxidatic mechanism of HProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Defining the binding determinants ofThe Journal of biological chemistry · 2018Article
- OxyR-regulated catalase CatB promotes the virulence in rice via detoxifying hydrogen peroxide in Xanthomonas oryzae pv. oryzae.BMC microbiology · 2016Article
- Elucidation of a mechanism of oxidative stress regulation in Francisella tularensis live vaccine strain.Molecular microbiology · 2016Article
- Corynebacterium diphtheriae putative tellurite-resistance protein (CDCE8392_0813) contributes to the intracellular survival in human epithelial cells and lethality of Caenorhabditis elegans.Memorias do Instituto Oswaldo Cruz · 2015Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Corynebacterium diphtheriae and Corynebacterium glutamicum each have one gene (cat) encoding catalase. In-frame Δcat mutants of C. diphtheriae and C. glutamicum were hyper-sensitive to growth inhibition and killing by H(2)O(2). In C. diphtheriae C7(β), both catalase activity and cat transcription decreased ~2-fold during transition from exponential growth to early stationary phase. Prototypic OxyR in Escherichia coli senses oxidative stress and it activates katG transcription and catalase production in response to H(2)O(2). In contrast, exposure of C. diphtheriae C7(β) to H(2)O(2) did not stimulate transcription of cat. OxyR from C. diphtheriae and C. glutamicum have 52% similarity with E. coli OxyR and contain homologs of the two cysteine residues involved in H(2)O(2) sensing by E. coli OxyR. In-frame ΔoxyR deletion mutants of C. diphtheriae C7(β), C. diphtheriae NCTC13129, and C. glutamicum were much more resistant than their parental wild type strains to growth inhibition by H(2)O(2). In the C. diphtheriae C7(β) ΔoxyR mutant, cat transcripts were about 8-fold more abundant and catalase activity was about 20-fold greater than in the C7(β) wild type strain. The oxyR gene from C. diphtheriae or C. glutamicum, but not from E. coli, complemented the defect in ΔoxyR mutants of C. diphtheriae and C. glutamicum and decreased their H(2)O(2) resistance to the level of their parental strains. Gel-mobility shift, DNaseI footprint, and primer extension assays showed that purified OxyR from C. diphtheriae C7(β) bound, in the presence or absence of DTT, to a sequence in the cat promoter region that extends from nucleotide position -55 to -10 with respect to the +1 nucleotide in the cat ORF. These results demonstrate that OxyR from C. diphtheriae or C. glutamicum functions as a transcriptional repressor of the cat gene by a mechanism that is independent of oxidative stress induced by H(2)O(2).
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