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• W2164453411 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." @default.
• W2164453411 created "2016-06-24" @default.
• W2164453411 creator A5016572389 @default.
• W2164453411 creator A5029976904 @default.
• W2164453411 date "2011-11-01" @default.
• W2164453411 modified "2023-10-07" @default.
• W2164453411 title "Bacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases" @default.
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• W2164453411 doi "https://doi.org/10.1099/mic.0.053579-0" @default.
• W2164453411 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3352277" @default.
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• W2164453411 hasPublicationYear "2011" @default.
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