Phylogeny of the α-crystallin-related heat-shock proteins

Nora Plesofsky-Vig, Jesse Vig, Robert Brambl

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57 Scopus citations

Abstract

Phylogenetic relationships were examined among 35 α-crystallin-related heat-shock proteins from animals, plants, and fungi. Approximately one-third of the aligned amino acids in these proteins were conserved in 74% of the proteins, and three blocks of consensus sequence were identified. Relationships were established by maximum parsimony and distance matrix analyses of the aligned amino acid sequences. The inferred phylogeny trees show the plant proteins clearly divided into three major groups that are unrelated to taxonomy: the chloroplast-localized proteins and two groups that originate from a common ancestral plant protein. The animal proteins, in contrast, branch in accordance with taxonomy, the only clear exception being the α-crystallin subgrouping of vertebrates. This analysis indicates that the small heat-shock proteins of animals have diverged more widely than have the plant proteins, one group of which is especially stable.

Original languageEnglish (US)
Pages (from-to)537-545
Number of pages9
JournalJournal of Molecular Evolution
Volume35
Issue number6
DOIs
StatePublished - Dec 1992

Keywords

  • Heat-shock proteins
  • Maximum parsimonx
  • Phylogeny
  • α-crystallin

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