Cambrian origin of the CYP27C1-mediated vitamin A 1 -to-A 2 switch, a key mechanism of vertebrate sensory plasticity
Author(s) -
Ala Morshedian,
Matthew B. Toomey,
Gabriel E. Pollock,
Rikard Frederiksen,
Jennifer M. Enright,
Stephen D. McCormick,
M. Carter Cornwall,
Gordon Fain,
Joseph C. Corbo
Publication year - 2017
Publication title -
royal society open science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.84
H-Index - 51
ISSN - 2054-5703
DOI - 10.1098/rsos.170362
Subject(s) - petromyzon , lamprey , vertebrate , biology , rhodopsin , evolutionary biology , opsin , spectral sensitivity , ecology , zoology , paleontology , retinal , genetics , botany , gene , wavelength , optoelectronics , physics
The spectral composition of ambient light varies across both space and time. Many species of jawed vertebrates adapt to this variation by tuning the sensitivity of their photoreceptors via the expression of CYP27C1, an enzyme that converts vitamin A 1 into vitamin A 2 , thereby shifting the ratio of vitamin A 1 -based rhodopsin to red-shifted vitamin A 2 -based porphyropsin in the eye. Here, we show that the sea lamprey ( Petromyzon marinus ), a jawless vertebrate that diverged from jawed vertebrates during the Cambrian period (approx. 500 Ma), dynamically shifts its photoreceptor spectral sensitivity via vitamin A 1 -to-A 2 chromophore exchange as it transitions between photically divergent aquatic habitats. We further show that this shift correlates with high-level expression of the lamprey orthologue of CYP27C1, specifically in the retinal pigment epithelium as in jawed vertebrates. Our results suggest that the CYP27C1-mediated vitamin A 1 -to-A 2 switch is an evolutionarily ancient mechanism of sensory plasticity that appeared not long after the origin of vertebrates.
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