ArticleJournal of bacteriology2002
Recognition of DNA by Fur: a reinterpretation of the Fur box consensus sequence.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.
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Who cites it
147 citing papers in PubMed, 281 citations in OpenAlex.
- Systematic characterization of PBP2 as the primary siderophore recognizer inMicrobial genomics · 2026Article
- Molecular Adaptations of Ferric Uptake Regulator (Fur) Proteins Drive Iron Homeostasis and Pathogenesis in Vibrio Spp.Current microbiology · 2026Review
- Iron-sulfur cluster biogenesis and regulation of intracellular iron homeostasis in Escherichia coli.Metallomics : integrated biometal science · 2025Review
- Functional Differentiation and Regulatory Mechanisms of Ferrochelatases HemH1 and HemH2 inInternational journal of molecular sciences · 2025Article
- Study in the iron uptake mechanism of Pasteurella multocida.Veterinary research · 2025Review
- Identification of a preferred DNA binding sequence and novel regulon member for CadR inFrontiers in microbiology · 2025Article
- Novel metal sites revealed by spectroscopic and structural characterization of the ferric uptake regulator fromComputational and structural biotechnology journal · 2025Article
- Cefiderocol Resistance Conferred by Plasmid-Located Ferric Citrate Transport System in KPC-Producing Klebsiella pneumoniae.Emerging infectious diseases · 2025Article
- Article
- Structural Perspectives on Metal Dependent Roles of Ferric Uptake Regulator (Fur).Biomolecules · 2024Review
- Siderophore-mediated iron acquisition byJournal of bacteriology · 2024Article
- The C-terminal domain of the ferric uptake regulator (Fur) binds a [2Fe-2S] cluster to sense the intracellular free iron content in Escherichia coli.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- Gut microbiomes of cycad-feeding insects tolerant to β-methylamino-L-alanine (BMAA) are rich in siderophore biosynthesis.ISME communications · 2023Article
- Functional Diversity of Homologous Oxidoreductases-Tuning of Substrate Specificity by a FAD-Stacking Residue for Iron Acquisition and Flavodoxin Reduction.Antioxidants (Basel, Switzerland) · 2023Article
- Ferric uptake regulator (Fur) binds a [2Fe-2S] cluster to regulate intracellular iron homeostasis in Escherichia coli.The Journal of biological chemistry · 2023Article
- Unusual Relationship between Iron Deprivation and Organophosphate Hydrolase Expression.Applied and environmental microbiology · 2023Article
- Meddling with Metal Sensors: Fur-Family Proteins as Signaling Hubs.Journal of bacteriology · 2023Review
- FoxR is an AraC-like transcriptional regulator of ferrioxamine uptake in Salmonella enterica.Molecular microbiology · 2022Article
- A single sensor controls large variations in zinc quotas in a marine cyanobacterium.Nature chemical biology · 2022Article
- The Burkholderia cenocepacia iron starvation σ factor, OrbS, possesses an on-board iron sensor.Nucleic acids research · 2022Article
87 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ferric uptake repressor (Fur) proteins regulate the expression of iron homeostasis genes in response to intracellular iron levels. In general, Fur proteins bind with high affinity to a 19-bp inverted repeat sequence known as the Fur box. An alignment of 19 operator sites recognized by Bacillus subtilis Fur revealed a different conserved 15-bp (7-1-7) inverted repeat present twice within this 19-bp consensus sequence. We demonstrated using electrophoretic mobility shift assays that this 7-1-7 inverted repeat comprises a minimal recognition site for high-affinity binding by Fur. The resulting revised consensus sequence is remarkably similar to a related 7-1-7 inverted repeat sequence recognized by PerR, a Fur paralog. Our analysis of the affinity and stoichiometry of DNA binding by B. subtilis Fur, together with a reinterpretation of previously described studies of Escherichia coli Fur, supports a model in which the 19-bp Fur box represents overlapping recognition sites for two Fur dimers bound to opposite faces of the DNA helix. The resulting recognition complex is reminiscent of that observed for the functionally related protein DtxR. Like Fur, DtxR contains a helix-turn-helix DNA-binding motif, recognizes a 19-bp inverted repeat sequence, and has a typical DNase I footprint of approximately 30 bp. By envisioning a similar mode of DNA recognition for Fur, we can account for the internal symmetries noted previously within the Fur box, the tendency of Fur to extend into adjacent regions of DNA in a sequence-selective manner, and the observed patterns of DNA protection against enzymatic and chemical probes.
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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.