ArticleNucleic acids research2015
Structural insight into operator dre-sites recognition and effector binding in the GntR/HutC transcription regulator NagR.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 47 citations in OpenAlex.
- NuConf: a rotamer library for DNA and RNA and its implementation in the protein design software MUMBO.Scientific reports · 2026Article
- The interaction between the RNA aptamer Dap1 and DasR mirrors DNA operator site recognition in GntR repressors.Nucleic acids research · 2026Article
- Molecular Strategies of Carbohydrate Binding to Intrinsically Disordered Regions in Bacterial Transcription Factors.International journal of molecular sciences · 2026Article
- FrlP, an ABC type I importer component ofJournal of bacteriology · 2025Article
- Molecular mechanisms underlying allosteric behavior of Escherichia coli DgoR, a GntR/FadR family transcriptional regulator.Nucleic acids research · 2025Article
- Synthetic biology design principles enable efficient bioproduction of Heparosan with low molecular weight and low polydispersion index for the biomedical industry.Synthetic biology (Oxford, England) · 2025Article
- Characterization of a widespread sugar phosphate-processing bacterial microcompartment.Communications biology · 2024Article
- Structural and Functional Characterization of Rv0792c from Mycobacterium tuberculosis: Identifying Small Molecule Inhibitor against HutC Protein.Microbiology spectrum · 2023Article
- NupR Responding to Multiple Signals Is a Nucleoside Permease Regulator in Bacillus thuringiensis BMB171.Microbiology spectrum · 2022Article
- Characterization of a Salmonella Transcription Factor-DNA Complex and Identification of the Inducer by Native Mass Spectrometry.Journal of molecular biology · 2022Article
- The Natural AntimicrobialFoods (Basel, Switzerland) · 2021Article
- Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism.Nature communications · 2021Article
- Design of a programmable biosensor-CRISPRi genetic circuits for dynamic and autonomous dual-control of metabolic flux in Bacillus subtilis.Nucleic acids research · 2020Article
- Bioremediation of a Common Product of Food Processing by a Human Gut Bacterium.Cell host & microbe · 2019Article
- Article
- Energy Transfer as A Driving Force in Nucleic Acid⁻Protein Interactions.Molecules (Basel, Switzerland) · 2019Article
- Molecular and Functional Insights into the Regulation of d-Galactonate Metabolism by the Transcriptional Regulator DgoR inJournal of bacteriology · 2019Article
- Cross Talk among Transporters of the Phosphoenolpyruvate-Dependent Phosphotransferase System in Bacillus subtilis.Journal of bacteriology · 2018Article
- Structural basis of effector and operator recognition by the phenolic acid-responsive transcriptional regulator PadR.Nucleic acids research · 2017Article
- Succinate production positively correlates with the affinity of the global transcription factor Cra for its effector FBP inBiotechnology for biofuels · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The uptake and metabolism of N-acetylglucosamine (GlcNAc) in Bacillus subtilis is controlled by NagR (formerly named YvoA), a member of the widely-occurring GntR/HutC family of transcription regulators. Upon binding to specific DNA operator sites (dre-sites) NagR blocks the transcription of genes for GlcNAc utilization and interaction of NagR with effectors abrogates gene repression. Here we report crystal structures of NagR in complex with operator DNA and in complex with the putative effector molecules glucosamine-6-phosphate (GlcN-6-P) and N-acetylglucosamine-6-phosphate (GlcNAc-6-P). A comparison of the distinct conformational states suggests that effectors are able to displace the NagR-DNA-binding domains (NagR-DBDs) by almost 70 Å upon binding. In addition, a high-resolution crystal structure of isolated NagR-DBDs in complex with palindromic double-stranded DNA (dsDNA) discloses both the determinants for highly sequence-specific operator dre-site recognition and for the unspecific binding of NagR to dsDNA. Extensive biochemical binding studies investigating the affinities of full-length NagR and isolated NagR-DBDs for either random DNA, dre-site-derived palindromic or naturally occurring non-palindromic dre-site sequences suggest that proper NagR function relies on an effector-induced fine-tuning of the DNA-binding affinities of NagR and not on a complete abrogation of its DNA binding.
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