ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure and regulon of Campylobacter jejuni ferric uptake regulator Fur define apo-Fur regulation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
85 citing papers in PubMed.
- Effects of RyhB on Fur regulation of cytochromeApplied and environmental microbiology · 2026Article
- Regulation of iron ion homeostasis inmBio · 2026Review
- Iron-sulfur cluster biogenesis and regulation of intracellular iron homeostasis in Escherichia coli.Metallomics : integrated biometal science · 2025Review
- Regulation of iron homeostasis by Fur and atypical response regulator SsoR via derepressor-inhibitor oscillation inApplied and environmental microbiology · 2025Article
- Temporal dynamics of gene expression during the development ofMicrobial genomics · 2025Article
- Novel metal sites revealed by spectroscopic and structural characterization of the ferric uptake regulator fromComputational and structural biotechnology journal · 2025Article
- Article
- Modelling protein complexes with crosslinking mass spectrometry and deep learning.Nature communications · 2024Article
- Structural Perspectives on Metal Dependent Roles of Ferric Uptake Regulator (Fur).Biomolecules · 2024Review
- Pleiotropic cellular responses underlying antibiotic tolerance inFrontiers in microbiology · 2024Article
- Proteomic analysis to unravel the biochemical mechanisms triggered by Bacillus toyonensis SFC 500-1E under chromium(VI) and phenol stress.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Review
- Ferric uptake regulator (Fur) binds a [2Fe-2S] cluster to regulate intracellular iron homeostasis in Escherichia coli.The Journal of biological chemistry · 2023Article
- Revisiting Fur Regulon Leads to a Comprehensive Understanding of Iron and Fur Regulation.International journal of molecular sciences · 2023Article
- Meddling with Metal Sensors: Fur-Family Proteins as Signaling Hubs.Journal of bacteriology · 2023Review
- Insights into the Orchestration of Gene Transcription Regulators inInternational journal of molecular sciences · 2022Review
- Article
- Ferrous Iron Uptake Is Required for Salmonella to Persist within Vacuoles of Host Cells.Infection and immunity · 2022Article
- Recent Advances in the Siderophore Biology ofFrontiers in microbiology · 2022Review
- Campylobacter jejuni genotypes are associated with post-infection irritable bowel syndrome in humans.Communications biology · 2021Article
- Transcription of Cystathionine β-Lyase (MetC) Is Repressed by HeuR in Campylobacter jejuni, and Methionine Biosynthesis Facilitates Colonocyte Invasion.Journal of bacteriology · 2021Article
25 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
The full regulatory potential of the ferric uptake regulator (Fur) family of proteins remains undefined despite over 20 years of study. We report herein an integrated approach that combines both genome-wide technologies and structural studies to define the role of Fur in Campylobacter jejuni (Cj). CjFur ChIP-chip assays identified 95 genomic loci bound by CjFur associated with functions as diverse as iron acquisition, flagellar biogenesis, and non-iron ion transport. Comparative analysis with transcriptomic data revealed that CjFur regulation extends beyond solely repression and also includes both gene activation and iron-independent regulation. Computational analysis revealed the presence of an elongated holo-Fur repression motif along with a divergent holo-Fur activation motif. This diversity of CjFur DNA-binding elements is supported by the crystal structure of CjFur, which revealed a unique conformation of its DNA-binding domain and the absence of metal in the regulatory site. Strikingly, our results indicate that the apo-CjFur structure retains the canonical V-shaped dimer reminiscent of previously characterized holo-Fur proteins enabling DNA interaction. This conformation stems from a structurally unique hinge domain that is poised to further contribute to CjFur's regulatory functions by modulating the orientation of the DNA-binding domain upon binding of iron. The unique features of the CjFur crystal structure rationalize the binding sequence diversity that was uncovered during ChIP-chip analysis and defines apo-Fur regulation.
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