ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural details of the OxyR peroxide-sensing mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed.
- Cysteine-based molecular switches: a focus on KEAP1 and BACH1 in regulating the antioxidant response.Archives of toxicology · 2026Review
- S267P mutation of OxyR regulator inSynthetic and systems biotechnology · 2026Article
- Endogenous Sulfane Sulfur Mediates the Oxidative Stress Response Process inAntioxidants (Basel, Switzerland) · 2026Article
- Mitigating protocatechuic acid toxicity in Vibrio natriegens enables poly-3-hydroxybutyrate production from an aromatic carbon source.Applied microbiology and biotechnology · 2026Article
- Monitoring in real time and far-red imaging of HNature chemical biology · 2026Article
- A color-tailored fluorogenic sensor for hydrogen peroxide.Nature chemical biology · 2026Article
- ROS-induced allosteric modulation of NikR promotesVirulence · 2025Article
- PexR is a noncanonical regulator of the peroxide stress response in bacteria.Nucleic acids research · 2025Article
- Modular evolution and regulatory diversification of nodD-like LysR-type transcriptional regulators in α-Proteobacteria.Archives of microbiology · 2025Article
- Systems-level exploitation of OxyR regulon unravels a potential antibacterial target in Pseudomonas aeruginosa.Communications biology · 2025Article
- Model organisms for investigating the functional involvement of NRF2 in non-communicable diseases.Redox biology · 2025Review
- Functional role of 18 LysR-Type transcriptional regulators of Salmonella enterica serovar Typhi.PloS one · 2025Article
- Fundamentals and Exceptions of the LysR-type Transcriptional Regulators.ACS synthetic biology · 2024Review
- OxyR is required for oxidative stress resistance of the entomopathogenic bacteriumMicrobiology (Reading, England) · 2024Article
- Structural and functional insights into transcription activation of the essential LysR-type transcriptional regulators.Protein science : a publication of the Protein Society · 2024Article
- Bacteria on the foundational kelp in kelp forest ecosystems: Insights from culturing, whole genome sequencing and metabolic assays.Environmental microbiology reports · 2024Article
- Ultra-fast genetically encoded sensor for precise real-time monitoring of physiological and pathophysiological peroxide dynamics.Research square · 2024Article
- Structure-guided engineering of a fast genetically encoded sensor for real-time HbioRxiv : the preprint server for biology · 2024Article
- Profiling of the Helicobacter pylori redox switch HP1021 regulon using a multi-omics approach.Nature communications · 2023Article
- Novel mechanism of hydrogen peroxide for promoting efficient natamycin synthesis inMicrobiology spectrum · 2023Article
23 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
OxyR, a bacterial peroxide sensor, is a LysR-type transcriptional regulator (LTTR) that regulates the transcription of defense genes in response to a low level of cellular H2O2. Consisting of an N-terminal DNA-binding domain (DBD) and a C-terminal regulatory domain (RD), OxyR senses H2O2 with conserved cysteine residues in the RD. However, the precise mechanism of OxyR is not yet known due to the absence of the full-length (FL) protein structure. Here we determined the crystal structures of the FL protein and RD of Pseudomonas aeruginosa OxyR and its C199D mutant proteins. The FL crystal structures revealed that OxyR has a tetrameric arrangement assembled via two distinct dimerization interfaces. The C199D mutant structures suggested that new interactions that are mediated by cysteine hydroxylation induce a large conformational change, facilitating intramolecular disulfide-bond formation. More importantly, a bound H2O2 molecule was found near the Cys199 site, suggesting the H2O2-driven oxidation mechanism of OxyR. Combined with the crystal structures, a modeling study suggested that a large movement of the DBD is triggered by structural changes in the regulatory domains upon oxidation. Taken together, these findings provide novel concepts for answering key questions regarding OxyR in the H2O2-sensing and oxidation-dependent regulation of antioxidant genes.
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