Phosphorylation of iodopsin, chicken red-sensitive cone visual pigment

Biochemistry. 1990 Oct 30;29(43):10102-6. doi: 10.1021/bi00495a013.

Abstract

The amino acid sequence has been determined for the carboxyl-terminal 41 amino acids of chicken red-sensitive cone pigment, iodopsin. This sequence is distinct from but structurally homologous to that of other visual pigments. It contains a region rich in the hydroxy amino acids serine and threonine. In the related rod cell visual pigment, rhodopsin, such serines and threonines have previously been identified as sites for phosphorylation by rhodopsin kinase. Phosphorylation of photolyzed rhodopsin serves to terminate its ability to function in visual transduction as an activator of G-protein. We have purified and reconstituted both chicken rhodopsin and chicken iodopsin and shown them to be phosphorylated by bovine rhodopsin kinase. Chicken iodopsin has a Km and Vmax similar to but distinguishably different from that for bovine rhodopsin. These results, in conjunction with other data, suggest that visual pigments in cone cells, upon absorption of light, undergo functional processes similar to those of the visual pigments in rod cells.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chickens
  • Eye Proteins*
  • G-Protein-Coupled Receptor Kinase 1
  • Kinetics
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Kinases / metabolism
  • Protein Processing, Post-Translational
  • Retinal Pigments / genetics
  • Retinal Pigments / metabolism*
  • Rhodopsin / metabolism
  • Rod Cell Outer Segment / metabolism
  • Rod Opsins*
  • Signal Transduction

Substances

  • Eye Proteins
  • Retinal Pigments
  • Rod Opsins
  • iodopsin
  • Rhodopsin
  • Protein Kinases
  • G-Protein-Coupled Receptor Kinase 1