The origins of novel protein interactions during animal opsin evolution.

Academic Article


  • BACKGROUND: Biologists are gaining an increased understanding of the genetic bases of phenotypic change during evolution. Nevertheless, the origins of phenotypes mediated by novel protein-protein interactions remain largely undocumented. METHODOLOGY/PRINCIPLE FINDINGS: Here we analyze the evolution of opsin visual pigment proteins from the genomes of early branching animals, including a new class of opsins from Cnidaria. We combine these data with existing knowledge of the molecular basis of opsin function in a rigorous phylogenetic framework. We identify adaptive amino acid substitutions in duplicated opsin genes that correlate with a diversification of physiological pathways mediated by different protein-protein interactions. CONCLUSIONS/SIGNIFICANCE: This study documents how gene duplication events early in the history of animals followed by adaptive structural mutations increased organismal complexity by adding novel protein-protein interactions that underlie different physiological pathways. These pathways are central to vision and other photo-reactive phenotypes in most extant animals. Similar evolutionary processes may have been at work in generating other metazoan sensory systems and other physiological processes mediated by signal transduction.
  • Authors

  • Plachetzki, David
  • Degnan, Bernard M
  • Oakley, Todd H
  • Publication Date

  • October 17, 2007
  • Published In

  • PLoS ONE  Journal
  • Keywords

  • Animals
  • Cnidaria
  • Evolution, Molecular
  • In Situ Hybridization
  • Light
  • Likelihood Functions
  • Markov Chains
  • Models, Biological
  • Phenotype
  • Phylogeny
  • Protein Interaction Mapping
  • Rod Opsins
  • Signal Transduction
  • Species Specificity
  • Digital Object Identifier (doi)

    Start Page

  • e1054
  • Volume

  • 2
  • Issue

  • 10