Cyp27c1 red-shifts the spectral sensitivity of photoreceptors by converting Vitamin A1 into A2

  • Jennifer M. Enright
  • , Matthew B. Toomey
  • , Shin Ya Sato
  • , Shelby E. Temple
  • , James R. Allen
  • , Rina Fujiwara
  • , Valerie M. Kramlinger
  • , Leslie D. Nagy
  • , Kevin M. Johnson
  • , Yi Xiao
  • , Martin J. How
  • , Stephen L. Johnson
  • , Nicholas W. Roberts
  • , Vladimir J. Kefalov
  • , F. Peter Guengerich
  • , Joseph C. Corbo

Research output: Contribution to journalArticlepeer-review

143 Scopus citations

Abstract

Some vertebrate species have evolved means of extending their visual sensitivity beyond the range of human vision. One mechanism of enhancing sensitivity to long-wavelength light is to replace the 11-cis retinal chromophore in photopigments with 11-cis 3,4-didehydroretinal. Despite over a century of research on this topic, the enzymatic basis of this perceptual switch remains unknown. Here, we show that a cytochrome P450 family member, Cyp27c1, mediates this switch by converting vitamin A1 (the precursor of 11-cis retinal) into vitamin A2 (the precursor of 11-cis 3,4-didehydroretinal). Knockout of cyp27c1 in zebrafish abrogates production of vitamin A2, eliminating the animal's ability to red-shift its photoreceptor spectral sensitivity and reducing its ability to see and respond to near-infrared light. Thus, the expression of a single enzyme mediates dynamic spectral tuning of the entire visual system by controlling the balance of vitamin A1 and A2 in the eye.

Original languageEnglish
Pages (from-to)3048-3057
Number of pages10
JournalCurrent Biology
Volume25
Issue number23
DOIs
StatePublished - Dec 7 2015

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