ArticleThe Journal of biological chemistry2009
Regulation of quinone oxidoreductase by the redox-sensing transcriptional regulator QorR in Corynebacterium glutamicum.
Article in The Journal of biological chemistry, 2009. 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, 47 citations in OpenAlex.
- Functional Identification of AcsR, a MarR Family Transcriptional Regulator Involved in the Regulation of Aromatic Compound-Degrading Genes inMicroorganisms · 2026Article
- Elucidating the Mechanism of Temporal Adaptation to Hydrogen Peroxide-Induced Oxidative Stress in Corynebacterium glutamicum.Microbial biotechnology · 2025Article
- SydR, a redox-sensing MarR-type regulator ofmBio · 2024Article
- The flavohaemoprotein hmp maintains redox homeostasis in response to reactive oxygen and nitrogen species in Corynebacterium glutamicum.Microbial cell factories · 2023Article
- OsnR is an autoregulatory negative transcription factor controlling redox-dependent stress responses in Corynebacterium glutamicum.Microbial cell factories · 2021Article
- The cssR gene of Corynebacterium glutamicum plays a negative regulatory role in stress responses.Microbial cell factories · 2021Article
- MsrR is a thiol-based oxidation-sensing regulator of the XRE family that modulates C. glutamicum oxidative stress resistance.Microbial cell factories · 2020Article
- The osnR gene of Corynebacterium glutamicum plays a negative regulatory role in oxidative stress responses.Journal of industrial microbiology & biotechnology · 2019Article
- OhsR acts as an organic peroxide-sensing transcriptional activator using an S-mycothiolation mechanism in Corynebacterium glutamicum.Microbial cell factories · 2018Article
- Thiol-based redox switches in prokaryotes.Biological chemistry · 2015Review
- Protein S-mycothiolation functions as redox-switch and thiol protection mechanism in Corynebacterium glutamicum under hypochlorite stress.Antioxidants & redox signaling · 2014Article
- Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR.Nucleic acids research · 2012Article
- Thiol-based redox switches and gene regulation.Antioxidants & redox signaling · 2011Review
- RosR (Cg1324), a hydrogen peroxide-sensitive MarR-type transcriptional regulator of Corynebacterium glutamicum.The Journal of biological chemistry · 2010Article
- The paralogous MarR/DUF24-family repressors YodB and CatR control expression of the catechol dioxygenase CatE in Bacillus subtilis.Journal of bacteriology · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Corynebacterium glutamicum cgR_1435 (cg1552) encodes a protein of the DUF24 protein family, which is a novel family of transcriptional regulators. CgR1435 (QorR) is a negative regulator of cgR_1436 (qor2), which is located upstream of cgR_1435 (qorR) in the opposite orientation, and its structural gene. QorR binds to the intergenic region between qor2 and qorR to repress their expression, which is induced by the thiol-specific oxidant diamide. The DNA-binding activity of QorR is impaired by oxidants such as diamide, H(2)O(2), and cumene hydroperoxide in vitro, and its lone cysteine residue (Cys-17) is essential for redox-responsive regulation of QorR activity both in vivo and in vitro. Moreover, a disruptant of qor2, which is a homologue of the ytfG gene of Escherichia coli encoding quinone oxidoreductase, shows increased sensitivity to diamide. It is concluded that the redox-sensing transcriptional regulator QorR is involved in disulfide stress response of C. glutamicum by regulating qor2 expression.
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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.