Roles of manganese and iron in the regulation of the biosynthesis of manganese-superoxide dismutase in Escherichia coli

FEMS Microbiol Rev. 1994 Aug;14(4):315-23. doi: 10.1111/j.1574-6976.1994.tb00105.x.

Abstract

Aerobic life-style offers both benefits and risks to living cells. The major risk comes from the formation of reactive oxygen intermediates (i.e. superoxide radical, O2-; hydrogen peroxide, H2O2; and hydroxyl radical, OH.) during normal oxygen metabolism. However, living cells are able to cope with oxygen toxicity by virtue of a unique set of antioxidant enzymes that scavenge O2- and H2O2, and prevent the formation OH.. Superoxide dismutases (SODs; EC 1.15.1.1) are metalloenzymes essential for aerobic survival. Escherichia coli contains two forms of this enzyme: an iron-containing enzyme (FeSOD) and a manganese-containing enzyme (MnSOD). In E. coli, MnSOD biosynthesis is under rigorous control. The enzyme is induced in response to a variety of environmental stress conditions including exposure to oxygen, redox cycling compounds such as paraquat which exacerbate the level of intracellular superoxide radicals, iron chelation (i.e. iron deprivation), and oxidants. A model for the regulation of the MnSOD has been proposed in which the MnSOD gene (sodA) is negatively regulated at the level of transcription by an iron-containing redox-sensitive repressor protein. The effect of iron-chelation most probably results in removal of the iron necessary for repressor activity. Recent studies have shown that sodA expression is regulated by three iron-dependent regulatory proteins, Fur (ferric uptake regulation), Fnr (fumarate nitrate regulation) and SoxR (superoxide regulon), and by the ArcA/ArcB (aerobic respiration control) system. The potential Fur-, Fnr- and ArcA-binding sites in the sodA promoter region have been identified by using different cis-acting regulatory mutations that caused anaerobic derepression of the gene.(ABSTRACT TRUNCATED AT 250 WORDS)

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / physiology
  • Base Sequence
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins*
  • Iron / pharmacology*
  • Iron-Sulfur Proteins*
  • Manganese / pharmacology*
  • Molecular Sequence Data
  • Repressor Proteins / physiology
  • Superoxide Dismutase / biosynthesis*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • FNR protein, E coli
  • Iron-Sulfur Proteins
  • Repressor Proteins
  • ferric uptake regulating proteins, bacterial
  • Manganese
  • Iron
  • Superoxide Dismutase