ArticleNucleic acids research2021
The bacterial iron sensor IdeR recognizes its DNA targets by indirect readout.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 15 citations in OpenAlex.
- Meta-analysis reveals a core iron-responsive gene signature in Mycobacterium tuberculosis linking siderophore biosynthesis, virulence, and metabolic adaptation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Pooled it
- Structural basis for transcription activation through cooperative recruitment of MntR.Nature communications · 2025Article
- Identification, characterization and classification of prokaryotic nucleoid-associated proteins.Molecular microbiology · 2025Review
- Iron, Copper, and Zinc Homeostasis in the Battle between Macrophage andCurrent medicinal chemistry · 2025Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- The molecular mechanisms of the bacterial iron sensor IdeR.Biochemical Society transactions · 2023Article
- Structural Dynamics of theInternational journal of molecular sciences · 2023Article
- The Iron Response ofFrontiers in cellular and infection microbiology · 2022Review
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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 iron-dependent regulator IdeR is the main transcriptional regulator controlling iron homeostasis genes in Actinobacteria, including species from the Corynebacterium, Mycobacterium and Streptomyces genera, as well as the erythromycin-producing bacterium Saccharopolyspora erythraea. Despite being a well-studied transcription factor since the identification of the Diphtheria toxin repressor DtxR three decades ago, the details of how IdeR proteins recognize their highly conserved 19-bp DNA target remain to be elucidated. IdeR makes few direct contacts with DNA bases in its target sequence, and we show here that these contacts are not required for target recognition. The results of our structural and mutational studies support a model wherein IdeR mainly uses an indirect readout mechanism, identifying its targets via the sequence-dependent DNA backbone structure rather than through specific contacts with the DNA bases. Furthermore, we show that IdeR efficiently recognizes a shorter palindromic sequence corresponding to a half binding site as compared to the full 19-bp target previously reported, expanding the number of potential target genes controlled by IdeR proteins.
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