ArticleThe Journal of biological chemistry2010
Heme-responsive DNA binding by the global iron regulator Irr from Rhizobium leguminosarum.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Antibacterial activity of green-synthesized silver nanoparticles against Gram-negative bacteria and insights into potential resistance mechanisms.INNOSC theranostics & pharmacological sciences · 2025Article
- Maintenance of heme homeostasis inJournal of bacteriology · 2023Article
- 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
- Article
- Bacterial iron detoxification at the molecular level.The Journal of biological chemistry · 2020Review
- Tuning the Binding Affinity of Heme-Responsive Biosensor for Precise and Dynamic Pathway Regulation.iScience · 2020Article
- Article
- Sensing iron availabilityChemical science · 2017Article
- Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017Review
- Metal-specific control of gene expression mediated by Bradyrhizobium japonicum Mur and Escherichia coli Fur is determined by the cellular context.Molecular microbiology · 2016Article
- A Heme-responsive Regulator Controls Synthesis of Staphyloferrin B in Staphylococcus aureus.The Journal of biological chemistry · 2016Article
- A bacterial iron exporter for maintenance of iron homeostasis.The Journal of biological chemistry · 2014Article
- Differential control of Bradyrhizobium japonicum iron stimulon genes through variable affinity of the iron response regulator (Irr) for target gene promoters and selective loss of activator function.Molecular microbiology · 2014Article
- The Porphyromonas gingivalis ferric uptake regulator orthologue binds hemin and regulates hemin-responsive biofilm development.PloS one · 2014Article
- The Mycobacterium tuberculosis secreted protein Rv0203 transfers heme to membrane proteins MmpL3 and MmpL11.The Journal of biological chemistry · 2013Article
- A model for tetrapyrrole synthesis as the primary mechanism for plastid-to-nucleus signaling during chloroplast biogenesis.Frontiers in plant science · 2013Article
- Bacterial iron-sulfur regulatory proteins as biological sensor-switches.Antioxidants & redox signaling · 2012Review
- Role of the Irr protein in the regulation of iron metabolism in Rhodobacter sphaeroides.PloS one · 2012Article
- The iron-responsive regulator irr is required for wild-type expression of the gene encoding the heme transporter BhuA in Brucella abortus 2308.Journal of bacteriology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Heme, a physiologically crucial form of iron, is a cofactor for a very wide range of proteins and enzymes. These include DNA regulatory proteins in which heme is a sensor to which an analyte molecule binds, effecting a change in the DNA binding affinity of the regulator. Given that heme, and more generally iron, must be carefully regulated, it is surprising that there are no examples yet in bacteria in which heme itself is sensed directly by a reversibly binding DNA regulatory protein. Here we show that the Rhizobium leguminosarum global iron regulatory protein Irr, which has many homologues within the alpha-proteobacteria and is a member of the Fur superfamily, binds heme, resulting in a dramatic decrease in affinity between the protein and its cognate, regulatory DNA operator sequence. Spectroscopic studies of wild-type and mutant Irr showed that the principal (but not only) heme-binding site is at a conserved HXH motif, whose substitution led to loss of DNA binding in vitro and of regulatory function in vivo. The R. leguminosarum Irr behaves very differently to the Irr of Bradyrhizobium japonicum, which is rapidly degraded in vivo by an unknown mechanism in conditions of elevated iron or heme, but whose DNA binding affinity in vitro does not respond to heme.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.