ArticleNucleic acids research2016
The activity of CouR, a MarR family transcriptional regulator, is modulated through a novel molecular mechanism.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 48 citations in OpenAlex.
- The MarR family regulator RmaH underlies the trade-off between acid sensitivity and antibiotic tolerance inJournal of bacteriology · 2026Article
- Precise Transcription Control Drives Optimized Catabolism of β-5-Type Lignin-Derived Dimers inJournal of agricultural and food chemistry · 2025Article
- Transcriptional regulation of two redundant 3-bromo-4-hydroxybenzoate catabolic operons via two different regulatory modes inApplied and environmental microbiology · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Quantitative Proteomics Analysis Reveals the Effect of a MarR Family Transcriptional RegulatorBiology · 2023Article
- MarR Family Transcriptional Regulators and Their Roles in Plant-Interacting Bacteria.Microorganisms · 2023Review
- AACS synthetic biology · 2022Article
- MdaB and NfrA, Two Novel Reductases Important in the Survival and Persistence of the Major Enteropathogen Campylobacter jejuni.Journal of bacteriology · 2022Article
- Characterization of the first tetrameric transcription factor of the GntR superfamily with allosteric regulation from the bacterial pathogen Agrobacterium fabrum.Nucleic acids research · 2021Article
- Re-engineering Plant Phenylpropanoid Metabolism With the Aid of Synthetic Biosensors.Frontiers in plant science · 2021Review
- A unified design allows fine-tuning of biosensor parameters and application across bacterial species.Metabolic engineering communications · 2020Article
- An alkaline active feruloyl-CoA synthetase from soil metagenome as a potential key enzyme for lignin valorization strategies.PloS one · 2019Article
- 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
- Copper (II) binding of NAD(P)H- flavin oxidoreductase (NfoR) enhances its Cr (VI)-reducing ability.Scientific reports · 2017Article
- Pseudomonas putida F1 uses energy taxis to sense hydroxycinnamic acids.Microbiology (Reading, England) · 2017Article
- Structural analysis of the regulatory mechanism of MarR protein Rv2887 in M. tuberculosis.Scientific reports · 2017Article
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- Regulation of Metabolic Pathways by MarR Family Transcription Factors.Computational and structural biotechnology journal · 2017Review
- Development and substrate specificity screening of an in vivo biosensor for the detection of biomass derived aromatic chemical building blocks.Chemical communications (Cambridge, England) · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
CouR, a MarR-type transcriptional repressor, regulates the cou genes, encoding p-hydroxycinnamate catabolism in the soil bacterium Rhodococcus jostii RHA1. The CouR dimer bound two molecules of the catabolite p-coumaroyl-CoA (Kd = 11 ± 1 μM). The presence of p-coumaroyl-CoA, but neither p-coumarate nor CoASH, abrogated CouR's binding to its operator DNA in vitro. The crystal structures of ligand-free CouR and its p-coumaroyl-CoA-bound form showed no significant conformational differences, in contrast to other MarR regulators. The CouR-p-coumaroyl-CoA structure revealed two ligand molecules bound to the CouR dimer with their phenolic moieties occupying equivalent hydrophobic pockets in each protomer and their CoA moieties adopting non-equivalent positions to mask the regulator's predicted DNA-binding surface. More specifically, the CoA phosphates formed salt bridges with predicted DNA-binding residues Arg36 and Arg38, changing the overall charge of the DNA-binding surface. The substitution of either arginine with alanine completely abrogated the ability of CouR to bind DNA. By contrast, the R36A/R38A double variant retained a relatively high affinity for p-coumaroyl-CoA (Kd = 89 ± 6 μM). Together, our data point to a novel mechanism of action in which the ligand abrogates the repressor's ability to bind DNA by steric occlusion of key DNA-binding residues and charge repulsion of the DNA backbone.
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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.