Iron and metal regulation in bacteria

Curr Opin Microbiol. 2001 Apr;4(2):172-7. doi: 10.1016/s1369-5274(00)00184-3.


In Escherichia coli, the iron regulator Fur is regulated by two oxidative-stress response regulators. The generation of dangerous radicals by oxygen and iron is the basis for this dual regulation, which is also found in eukaryotes. The binding of iron-regulated transcripts to apo-aconitase and results of mRNA half-life studies indicate that there is post-transcriptional iron regulation in bacteria, as in eukaryotes. Fur contains two metal-binding sites, one for Zn2+ and one for Fe2+. Zinc uptake systems are regulated by members of the Fur protein family, and zinc is a cofactor. DtxR and related proteins constitute another family of iron regulators, first found in Gram-positive organisms with a high GC content. In organisms with Fur-dependent iron regulation, members of the DtxR family regulate manganese transport.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Aconitate Hydratase / genetics
  • Aconitate Hydratase / metabolism
  • Bacteria / genetics*
  • Bacteria / metabolism*
  • Bacterial Proteins / metabolism*
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression Regulation, Bacterial*
  • Iron / metabolism*
  • Manganese / metabolism
  • RNA Processing, Post-Transcriptional
  • Repressor Proteins / metabolism*
  • Siderophores / genetics
  • Siderophores / metabolism
  • Transcription, Genetic
  • Zinc / metabolism


  • Bacterial Proteins
  • DNA-Binding Proteins
  • DtxR protein, Corynebacterium diphtheriae
  • Repressor Proteins
  • Siderophores
  • ferric uptake regulating proteins, bacterial
  • Manganese
  • Iron
  • Aconitate Hydratase
  • Zinc