1887

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 , 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 (formerly ), 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. also encodes an IsdG family protein designated HmoB (formerly YhgC). Unlike , is constitutively expressed and not under Fur control. HmoA and HmoB both bind haemin 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 can use haem as an iron source, but that this ability is independent of HmoA and HmoB.

Funding
This study was supported by the:
  • National Institutes of Health (Award GM059323)
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2011-11-01
2022-01-22
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