ArticleScientific reports2016
The solution configurations of inactive and activated DntR have implications for the sliding dimer mechanism of LysR transcription factors.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Symmetric Dimeric Structure and Ligand Recognition of CutR, a LysR-Type Transcriptional Regulator fromInternational journal of molecular sciences · 2025Article
- Mutation ofAntibiotics (Basel, Switzerland) · 2025Article
- Transcriptional regulation of two redundant 3-bromo-4-hydroxybenzoate catabolic operons via two different regulatory modes inApplied and environmental microbiology · 2025Article
- A bacterial transcription activator dedicated to the expression of the enzyme catalyzing the first committed step in fatty acid biosynthesis.Nucleic acids research · 2024Article
- Fundamentals and Exceptions of the LysR-type Transcriptional Regulators.ACS synthetic biology · 2024Review
- Structural and functional insights into transcription activation of the essential LysR-type transcriptional regulators.Protein science : a publication of the Protein Society · 2024Article
- Precise Regulation of Differential Transcriptions of Various Catabolic Genes by OdcR via a Single Nucleotide Mutation in the Promoter Ensures the Safety of Metabolic Flux.Applied and environmental microbiology · 2022Article
- Regulation of l- and d-Aspartate Transport and Metabolism in Acinetobacter baylyi ADP1.Applied and environmental microbiology · 2022Article
- Functional and structural analysis of catabolite control protein C that responds to citrate.Scientific reports · 2021Article
- The LysR-Type Transcriptional Regulator BsrA (PA2121) Controls Vital Metabolic Pathways inmSystems · 2021Article
- Similar solutions to a common challenge: regulation of genes encoding Ralstonia solanacearum xanthine dehydrogenase.FEMS microbiology letters · 2021Article
- Characterization of the pleiotropic LysR-type transcription regulator LeuO of Escherichia coli.Nucleic acids research · 2019Article
- Engineering CatM, a LysR-Type Transcriptional Regulator, to Respond Synergistically to Two Effectors.Genes · 2019Article
- A novel 3-hydroxypropionic acid-inducible promoter regulated by the LysR-type transcriptional activator protein MmsR of Pseudomonas denitrificans.Scientific reports · 2019Article
- Development of Aspirin-Inducible Biosensors inApplied and environmental microbiology · 2019Article
- DbdR, a New Member of the LysR Family of Transcriptional Regulators, Coordinately Controls Four Promoters in the Thauera aromatica AR-1 3,5-Dihydroxybenzoate Anaerobic Degradation Pathway.Applied and environmental microbiology · 2019Article
- Variants of theFrontiers in microbiology · 2019Article
- Crystal structure of the ligand-binding domain of a LysR-type transcriptional regulator: transcriptional activation via a rotary switch.Molecular microbiology · 2018Article
- Cell-Wall Recycling of the Gram-Negative Bacteria and the Nexus to Antibiotic Resistance.Chemical reviews · 2018Review
- Coordinating carbon and nitrogen metabolic signaling through the cyanobacterial global repressor NdhR.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LysR Type Transcriptional Regulators (LTTRs) regulate basic metabolic pathways or virulence gene expression in prokaryotes. Evidence suggests that the activation of LTTRs involves a conformational change from an inactive compact apo- configuration that represses transcription to an active, expanded holo- form that promotes it. However, no LTTR has yet been observed to adopt both configurations. Here, we report the results of structural studies of various forms of the LTTR DntR. Crystal structures of apo-DntR and of a partially autoinducing mutant H169T-DntR suggest that active and inactive DntR maintain a compact homotetrameric configuration. However, Small Angle X-ray Scattering (SAXS) studies on solutions of apo-, H169T- and inducer-bound holo-DntR indicate a different behaviour, suggesting that while apo-DntR maintains a compact configuration in solution both H169T- and holo-DntR adopt an expanded conformation. Models of the SAXS-obtained solution conformations of apo- and holo-DntR homotetramers in complex with promoter-operator region DNA are consistent with previous observations of a shifting of LTTR DNA binding sites upon activation and a consequent relaxation in the bend of the promoter-operator region DNA. Our results thus provide clear evidence at the molecular level which strongly supports the 'sliding dimer' hypothesis concerning LTTR activation mechanisms.
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