Metallothionein primary structure in amphibians: Insights from comparative evolutionary analysis in vertebrates

C R Biol. 2012 Jul;335(7):480-7. doi: 10.1016/j.crvi.2012.05.003. Epub 2012 Jun 17.

Abstract

Metallothioneins are cysteine-rich, low-molecular weight metal-binding proteins ubiquitously expressed in living organisms. In the last past years, the increasing amount of vertebrate non-mammalian metallothionein sequences available have disclosed for these proteins differences in the primary structure that have not been supposed before. To provide a more up-to-date view of the metallothioneins in non-mammalian tetrapods, we decided to increase the still scarce knowledge concerning the primary structure and the evolution of metallothioneins in amphibians. Our data demonstrate an unexpected diversity of metallothionein sequences among amphibians, accompanied by remarkable features in their phylogeny. Phylogenetic analysis also reveals the complexity of vertebrate metallothionein evolution, made by both ancient and more recent events of gene duplication and loss.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Evolution, Molecular
  • Gene Duplication
  • Hydrophobic and Hydrophilic Interactions
  • Likelihood Functions
  • Metallothionein / chemistry*
  • Metallothionein / genetics
  • Molecular Sequence Data
  • Phylogeny
  • Protein Conformation
  • Rana esculenta / genetics*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Triturus / genetics*
  • Vertebrates / genetics

Substances

  • Metallothionein

Associated data

  • GENBANK/HE681911
  • GENBANK/HE681912