Molecular evolution of peptide methionine sulfoxide reductases (MsrA and MsrB): on the early development of a mechanism that protects against oxidative damage

J Mol Evol. 2007 Jan;64(1):15-32. doi: 10.1007/s00239-005-0281-2. Epub 2006 Dec 18.

Abstract

Methionine sulfoxide reductases, enzymes that reverse the oxidation of methionine residues, have been described in a wide range of species. The reduction of the diastereoisomers of oxidized methionine is catalyzed by two different monomeric methionine sulfoxide reductases (MsrA and MsrB) and is best understood as an evolutionary response to high levels of oxygen either in the Earth's atmosphere or possibly in more localized environments. Phylogenetic analyses of these proteins suggest that their distribution is the outcome of a complex history including many paralogy and lateral gene transfer events.

MeSH terms

  • Animals
  • Bacterial Proteins / physiology
  • Evolution, Molecular*
  • Humans
  • Methionine Sulfoxide Reductases
  • Microfilament Proteins
  • Oxidative Stress
  • Oxidoreductases / physiology*
  • Phylogeny*
  • RNA, Ribosomal, 16S
  • RNA, Ribosomal, 18S
  • Symbiosis
  • Transcription Factors

Substances

  • Bacterial Proteins
  • Microfilament Proteins
  • RNA, Ribosomal, 16S
  • RNA, Ribosomal, 18S
  • Transcription Factors
  • Oxidoreductases
  • MSRB2 protein, human
  • Methionine Sulfoxide Reductases
  • methionine sulfoxide reductase