Evolution under pressure and the adaptation of visual pigment compressibility in deep-sea environments

Megan L. Porter, Nicholas W. Roberts*, Julian C. Partridge

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

4 Citations (Scopus)
306 Downloads (Pure)


Understanding the link between how proteins function in animals that live in extreme environments and selection on specific properties of amino acids has proved extremely challenging. Here we present the discovery of how the compressibility of opsin proteins in two evolutionarily distinct animal groups, teleosts and cephalopods, appears to be adapted to the high-pressure environment of the deep-sea. We report how in both groups, opsins in deeper living species are calculated to be less compressible. This is largely due to a common set of amino acid sites (bovRH#159, 196, 213, 275) undergoing positive destabilizing selection in six of the twelve amino acid physiochemical properties that determine protein compressibility. This suggests a common evolutionary mechanism to reduce the adiabatic compressibility of opsin proteins. Intriguingly, the sites under selection are on the proteins’ outer faces at locations known to be involved in opsin-opsin dimer interactions.
Original languageEnglish
Pages (from-to)160-165
Number of pages6
JournalMolecular Phylogenetics and Evolution
Early online date12 Aug 2016
Publication statusPublished - 1 Dec 2016


  • Opsin
  • Evolution
  • Deep-sea
  • Compressibility
  • Teleost
  • Cephalopod

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