ArticleMolecular microbiology2015
The mycobacterial iron-dependent regulator IdeR induces ferritin (bfrB) by alleviating Lsr2 repression.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- DtxR is a global iron-dependent regulatory protein with multiple roles in the control of gene expression inJournal of bacteriology · 2026Article
- Molecular Kaleidoscope of Nucleoid-Associated Proteins Regulatory Network and Chromosome Architecture in Mycobacterium Tuberculosis.Current microbiology · 2026Review
- Retro-inversion imparts antimycobacterial specificity to host defense peptides.Nature communications · 2025Article
- NapR Regulates the Expression of Phosphoserine Aminotransferase SerC to Modulate Biofilm Formation and Resistance to Serine Stress of Mycobacteria.International journal of molecular sciences · 2025Article
- Iron, Copper, and Zinc Homeostasis in the Battle between Macrophage andCurrent medicinal chemistry · 2025Review
- The role of transcriptional regulators in metal ion homeostasis ofFrontiers in cellular and infection microbiology · 2024Review
- The progress ofFrontiers in medicine · 2024Review
- TargetingRSC medicinal chemistry · 2023Review
- The molecular mechanisms of the bacterial iron sensor IdeR.Biochemical Society transactions · 2023Article
- Ferritin from Mycobacterium abscessus is involved in resistance to antibiotics and oxidative stress.Applied microbiology and biotechnology · 2023Article
- Immunobiology of tubercle bacilli and prospects of immunomodulatory drugs to tackle tuberculosis (TB) and other non-tubercular mycobacterial infections.Immunobiology · 2022Review
- The Iron Response ofFrontiers in cellular and infection microbiology · 2022Review
- The bacterial iron sensor IdeR recognizes its DNA targets by indirect readout.Nucleic acids research · 2021Article
- Article
- Co-infections as Modulators of Disease Outcome: Minor Players or Major Players?Frontiers in microbiology · 2021Review
- Survival in Hostile Conditions: Pupylation and the Proteasome in Actinobacterial Stress Response Pathways.Frontiers in molecular biosciences · 2021Review
- Article
- Silencing cryptic specialized metabolism ineLife · 2019Article
- Iron and Zinc Regulate Expression of a Putative ABC Metal Transporter in Corynebacterium diphtheriae.Journal of bacteriology · 2018Article
- Role of Bacterioferritin & Ferritin inFrontiers in cellular and infection microbiology · 2017Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Emerging evidence indicates that precise regulation of iron (Fe) metabolism and maintenance of Fe homeostasis in Mycobacterium tuberculosis (Mtb) are essential for its survival and proliferation in the host. IdeR is a central transcriptional regulator of Mtb genes involved in Fe metabolism. While it is well understood how IdeR functions as a repressor, how it induces transcription of a subset of its targets is still unclear. We investigated the molecular mechanism of IdeR-mediated positive regulation of bfrB, the gene encoding the major Fe-storage protein of Mtb. We found that bfrB induction by Fe required direct interaction of IdeR with a DNA sequence containing four tandem IdeR-binding boxes located upstream of the bfrB promoter. Results of in vivo and in vitro transcription assays identified a direct repressor of bfrB, the histone-like protein Lsr2. IdeR counteracted Lsr2-mediated repression in vitro, suggesting that IdeR induces bfrB transcription by antagonizing the repressor activity of Lsr2. Together, these results elucidate the main mechanism of bfrB positive regulation by IdeR and identify Lsr2 as a new factor contributing to Fe homeostasis in mycobacteria.
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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.