ArticleMicrobiology (Reading, England)2011
Bacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases.
Article in Microbiology (Reading, England), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 20 citations in OpenAlex.
- Metabolic engineering ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Iron Deficiency Response of Corynebacterium glutamicum and a Link to Thiamine Biosynthesis.Applied and environmental microbiology · 2020Article
- Heme catabolism in the causative agent of anthrax.Molecular microbiology · 2019Article
- Intracellular Zn(II) Intoxication Leads to Dysregulation of the PerR Regulon Resulting in Heme Toxicity in Bacillus subtilis.PLoS genetics · 2016Article
- Global Transcriptional Analysis of Virus-Host Interactions between Phage ϕ29 and Bacillus subtilis.Journal of virology · 2016Article
- Reconstruction of the Regulatory Network for Bacillus subtilis and Reconciliation with Gene Expression Data.Frontiers in microbiology · 2016Article
- Transcriptomic and phenotypic analysis of paralogous spx gene function in Bacillus anthracis Sterne.MicrobiologyOpen · 2013Article
- Staphylococcus aureus FepA and FepB proteins drive heme iron utilization in Escherichia coli.PloS one · 2013Article
- Structure of the signal transduction protein TRAP (target of RNAIII-activating protein).Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Derepression of the Bacillus subtilis PerR peroxide stress response leads to iron deficiency.Journal of bacteriology · 2012Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Identification of genes regulated by the ferric uptake regulator (Fur) protein has provided insights into the diverse mechanisms of adaptation to iron limitation. In the soil bacterium Bacillus subtilis, Fur senses iron sufficiency and represses genes that enable iron uptake, including biosynthetic and transport genes for the siderophore bacillibactin and uptake systems for siderophores produced by other organisms. We here demonstrate that Fur regulates hmoA (formerly yetG), which encodes a haem monooxygenase. HmoA is the first characterized member of a divergent group of putative monooxygenases that cluster separately from the well-characterized IsdG family. B. subtilis also encodes an IsdG family protein designated HmoB (formerly YhgC). Unlike hmoA, hmoB is constitutively expressed and not under Fur control. HmoA and HmoB both bind haemin in vitro with approximately 1 : 1 stoichiometry and degrade haemin in the presence of an electron donor. Mutational and spectroscopic analyses indicate that HmoA and HmoB have distinct active site architectures and interact differently with haem. We further show that B. subtilis can use haem as an iron source, but that this ability is independent of HmoA and HmoB.
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