ArticleThe Journal of biological chemistry2016
Molecular Insights into the Impact of Oxidative Stress on the Quorum-Sensing Regulator Protein LasR.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- You Talking to Me? Quorum Sensing in Symbiotic Microbes and Their Response to Environmental Variation.Microorganisms · 2026Review
- Inhibition of acyl-homoserine-lactone synthase inIn silico pharmacology · 2025Article
- Development and Characterization of LasR Immobilized Monolithic Column for Screening Active Ingredients as Quorum Sensing Inhibitors AgainstDrug design, development and therapy · 2025Article
- The transcriptional regulators of virulence forGenes & diseases · 2023Review
- Article
- Inhibition of Quorum-Sensing Regulator fromMolecules (Basel, Switzerland) · 2022Article
- A Commensal Streptococcus Dysregulates theFrontiers in cellular and infection microbiology · 2022Article
- Sulfane Sulfur Regulates LasR-Mediated Quorum Sensing and Virulence inAntioxidants (Basel, Switzerland) · 2021Article
- Oxidative Stress Response inPathogens (Basel, Switzerland) · 2021Review
- Article
- Allelic polymorphism shapes community function in evolving Pseudomonas aeruginosa populations.The ISME journal · 2020Article
- Modulation ofJournal of bacteriology · 2019Article
- N-dodecanoyl-homoserine lactone influences the levels of thiol and proteins related to oxidation-reduction process in Salmonella.PloS one · 2018Article
- Molecular Insights into Hydrogen Peroxide-sensing Mechanism of the Metalloregulator MntR in Controlling Bacterial Resistance to Oxidative Stresses.The Journal of biological chemistry · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The LasR regulator protein functions at the top of the Pseudomonas aeruginosa quorum-sensing hierarchy and is implicated in promoting bacterial virulence. Of note is recent evidence that this transcription factor may also respond to oxidative stress. Here, all cysteines in LasR were inspected to deduce their redox sensitivity and to probe the connection between stress response and LasR activity using purified LasR and individual LasR domains. Cys(79) in the ligand binding domain of LasR appears to be important for ligand recognition and folding of this domain to potentiate DNA binding but does not seem to be sensitive to oxidative stress when bound to its native ligand. Two cysteines in the DNA binding domain of LasR do form a disulfide bond when treated with hydrogen peroxide, and formation of this Cys(201)-Cys(203) disulfide bond appears to disrupt the DNA binding activity of the transcription factor. Mutagenesis of either of these cysteines leads to expression of a protein that no longer binds DNA. A cell-based reporter assay linking LasR function with β-galactosidase activity gave results consistent with those obtained with purified LasR. This work provides a possible mechanism for oxidative stress response by LasR and indicates that multiple cysteines within the protein may prove to be useful targets for disabling its activity.
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