ArticleProceedings of the National Academy of Sciences of the United States of America1999
Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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74 citing papers in PubMed, 166 citations in OpenAlex.
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- Functional versatility of Zur in metal homeostasis, motility, biofilm formation, and stress resistance inMicrobiology spectrum · 2024Article
- Scanning iron response regulator binding sites using Dap-seq in the Brucella genome.PLoS neglected tropical diseases · 2023Article
- A haem-sequestering plant peptide promotes iron uptake in symbiotic bacteria.Nature microbiology · 2022Article
- Regulation of protein function and degradation by heme, heme responsive motifs, and CO.Critical reviews in biochemistry and molecular biology · 2022Review
- The FUR-like regulators PerRA and PerRB integrate a complex regulatory network that promotes mammalian host-adaptation and virulence of Leptospira interrogans.PLoS pathogens · 2021Article
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- Bacterial iron detoxification at the molecular level.The Journal of biological chemistry · 2020Review
- Symbiosis, virulence and natural-product biosynthesis in entomopathogenic bacteria are regulated by a small RNA.Nature microbiology · 2020Article
- Mechanistic insights into heme-mediated transcriptional regulation via a bacterial manganese-binding iron regulator, iron response regulator (Irr).The Journal of biological chemistry · 2020Article
- HrrSA orchestrates a systemic response to heme and determines prioritization of terminal cytochrome oxidase expression.Nucleic acids research · 2020Article
- Tuning the Binding Affinity of Heme-Responsive Biosensor for Precise and Dynamic Pathway Regulation.iScience · 2020Article
- "Labile" heme critically regulates mitochondrial biogenesis through the transcriptional co-activator Hap4p inThe Journal of biological chemistry · 2020Article
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- Ecological Conditions and Molecular Determinants Involved inFrontiers in plant science · 2019Review
- Redox Regulation of Heme Oxygenase-2 and the Transcription Factor, Rev-Erb, Through Heme Regulatory Motifs.Antioxidants & redox signaling · 2018Review
- Sensing iron availabilityChemical science · 2017Article
- BosR Is A Novel Fur Family Member Responsive to Copper and Regulating Copper Homeostasis in Borrelia burgdorferi.Journal of bacteriology · 2017Article
- The heme-regulatory motif of nuclear receptor Rev-erbβ is a key mediator of heme and redox signaling in circadian rhythm maintenance and metabolism.The Journal of biological chemistry · 2017Article
14 more citing papers are in PubMed but not listed here.
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial iron response regulator (Irr) protein mediates iron-dependent regulation of heme biosynthesis. Pulse-chase and immunoprecipitation experiments showed that Irr degraded in response to 6 microM iron with a half-life of approximately 30 min and that this regulated stability was the principal determinant of control by iron. Irr contains a heme regulatory motif (HRM) near its amino terminus. A role for heme in regulation was implicated by the retention of Irr in heme synthesis mutants in the presence of iron. Addition of heme to low iron (0.3 microM) cultures was sufficient for the disappearance of Irr in cells of the wild-type and heme mutant strains. Spectral and binding analyses of purified recombinant Irr showed that the protein bound heme with high affinity and caused a blue shift in the absorption spectrum of heme to a shorter wavelength. A Cys(29) --> Ala substitution within the HRM of Irr (IrrC29A) abrogated both high affinity binding to heme and the spectral blue shift. In vivo turnover experiments showed that, unlike wild-type Irr, IrrC29A was stable in the presence of iron. We conclude that iron-dependent degradation of Irr involves direct binding of heme to the protein at the HRM. The findings implicate a regulatory role for heme in protein degradation and provide direct evidence for a functional HRM in a prokaryote.
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