ArticleJournal of bacteriology2013
Mutational analysis of the multiple-antibiotic resistance regulator MarR reveals a ligand binding pocket at the interface between the dimerization and DNA binding domains.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 46 citations in OpenAlex.
- TagR, a newly identified member of the MarR family of transcriptional regulators, represses the NRPS operon inMicrobiology spectrum · 2026Article
- Highly Drug-Resistant Escherichia coli from Hospital Wastewater with Several Evolutionary Mutations: An Integrated Insights from Molecular, Computational, and Biophysics.Molecular biotechnology · 2026Article
- Paeonol eradicates biofilm in porcine-source Escherichia coli by targeting the quorum sensing system.BMC veterinary research · 2025Article
- The MarR family transcription factor SlyA senses iron and respiratory status in enteric bacteria.mBio · 2025Article
- MexR and NalD are pyocyanin-responsive transcriptional repressors of the efflux pump MexAB-OprM in Pseudomonas aeruginosa.Nucleic acids research · 2025Article
- Aspirin-responsive gene switch regulating therapeutic protein expression.Nature communications · 2025Article
- Targeting MarA N-terminal domain dynamics to prevent DNA binding.Protein science : a publication of the Protein Society · 2025Article
- Structural basis of transcriptional regulation by UrtR in response to uric acid.Nucleic acids research · 2024Article
- Review
- RND Efflux Pump Induction: A Crucial Network Unveiling Adaptive Antibiotic Resistance Mechanisms of Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2024Review
- The Mar, Sox, and Rob Systems.EcoSal Plus · 2023Review
- Design and characterization of a salicylic acid-inducible gene expression system for Jurkat cells.Journal of biotechnology · 2022Article
- Development and selection of low-level multi-drug resistance over an extended range of sub-inhibitory ciprofloxacin concentrations in Escherichia coli.Scientific reports · 2020Article
- Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Escherichia coli MarA protein regulates the ycgZ-ymgABC operon to inhibit biofilm formation.Molecular microbiology · 2019Article
- Rapid decline of bacterial drug-resistance in an antibiotic-free environment through phenotypic reversion.eLife · 2019Article
- Article
- Cross Talk between MarR-Like Transcription Factors Coordinates the Regulation of Motility in Uropathogenic Escherichia coli.Infection and immunity · 2018Article
- Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator.eLife · 2018Article
- Structural basis of transcriptional regulation by CouR, a repressor of coumarate catabolism, inThe Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The Escherichia coli regulator MarR represses the multiple-antibiotic resistance operon marRAB and responds to phenolic compounds, including sodium salicylate, which inhibit its activity. Crystals obtained in the presence of a high concentration of salicylate indicated two possible salicylate sites, SAL-A and SAL-B. However, it was unclear whether these sites were physiologically significant or were simply a result of the crystallization conditions. A study carried out on MarR homologue MTH313 suggested the presence of a salicylate binding site buried at the interface between the dimerization and the DNA-binding domains. Interestingly, the authors of the study indicated a similar pocket conserved in the MarR structure. Since no mutagenesis analysis had been performed to test which amino acids were essential in salicylate binding, we examined the role of residues that could potentially interact with salicylate. We demonstrated that mutations in residues shown as interacting with salicylate at SAL-A and SAL-B in the MarR-salicylate structure had no effect on salicylate binding, indicating that these sites were not the physiological regulatory sites. However, some of these residues (P57, R86, M74, and R77) were important for DNA binding. Furthermore, mutations in residues R16, D26, and K44 significantly reduced binding to both salicylate and 2,4-dinitrophenol, while a mutation in residue H19 impaired the binding to 2,4-dinitrophenol only. These findings indicate, as for MTH313, the presence of a ligand binding pocket located between the dimerization and DNA binding domains.
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Registered trials
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