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Evolution of nonspectral rhodopsin function at high altitudes.

Gianni M Castiglione1,2, Frances E Hauser2, Brian S Liao1

  • 1Department of Cell & Systems Biology, University of Toronto, Toronto, ON, Canada M5S 3G5.

Proceedings of the National Academy of Sciences of the United States of America
|June 24, 2017
PubMed
Summary
This summary is machine-generated.

High-altitude fish exhibit cold-adapted rhodopsin (RH1), a visual pigment. Unique amino acid changes in RH1 enhance function in cold, low-oxygen mountain waters.

Keywords:
Andean catfishesG protein-coupled receptorin vitro expressionprotein evolutionvisual pigment

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Area of Science:

  • Evolutionary Biology
  • Biochemistry
  • Physiology

Background:

  • High-altitude environments pose physiological challenges like low oxygen and temperatures.
  • While terrestrial animals show protein adaptations, aquatic ectotherm adaptations are less understood.
  • Signaling proteins, like G protein-coupled receptors (GPCRs), may vary with temperature.

Purpose of the Study:

  • Investigate rhodopsin (RH1) evolution and cold adaptation in Andean mountain catfish.
  • Understand thermal adaptation mechanisms in GPCRs using RH1 as a model.

Main Methods:

  • Molecular evolutionary analyses to identify adaptive sites in RH1.
  • Site-directed mutagenesis to test the function of high-altitude RH1 variants.
  • Biochemical assays to assess rhodopsin stability and kinetics.

Main Results:

  • Identified unique amino acid substitutions under positive selection in high-altitude catfish RH1.
  • Mutagenesis revealed these substitutions decrease rhodopsin stability but accelerate ligand-bound form decay.
  • This phenotype likely counteracts cold-induced kinetic rate reductions.

Conclusions:

  • Rhodopsin (RH1) shows evidence of cold adaptation in high-altitude fish.
  • Natural variation in GPCRs can enhance function in cold environments.
  • Findings contribute to understanding visual pigment adaptation to extreme environments.