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PMID: 15851682 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

A rhodopsin exhibiting binding ability to agonist all-trans-retinal.

Tsukamoto H, Terakita A, Shichida Y

Abstract

Rhodopsins are the members of the family of G protein-coupled receptors that have diverged from ligand-binding receptors into photoreceptive pigments. Vertebrate rhodopsins are able to bind the inverse agonist 11-cis-retinal but are unable to bind the agonist all-trans-retinal, indicating that vertebrate rhodopsin changed its binding ability during the course of molecular evolution. Here, we show that unlike vertebrate rhodopsin, amphioxus rhodopsin is still able to bind the agonist all-trans-retinal. The opsin of amphioxus rhodopsin can also bind 11-cis-retinal to form a photoreceptive pigment that can convert to a red-shifted photoproduct through cis-trans isomerization of the chromophore upon photon absorption. The red-shifted photoproduct is the stable G protein activating state. Incubation of the opsin with all-trans-retinal produces a G protein activating state that is spectroscopically and biochemically indistinguishable from the red-shifted photoproduct, indicating that the opsin possesses agonist-binding ability. The opsin exhibits an approximately 50-fold higher affinity for 11-cis-retinal than for all-trans-retinal, and mutational analyses revealed that Trp-265 situated in helix VI is important for the increase in binding affinity to 11-cis-retinal. These properties of amphioxus rhodopsin suggest that an ancestral rhodopsin increased the affinity for 11-cis-retinal by rearrangement of a structure including Trp-265 to act as a photoreceptor. In addition, an additional mechanism was acquired in vertebrate rhodopsin to prevent completely the binding of exogenous all-trans-retinal during molecular evolution.

MeSH Terms
Animals Binding, Competitive/physiology Chordata, Nonvertebrate/metabolism Chromatography, High Pressure Liquid Evolution, Molecular GTP-Binding Proteins/metabolism Photochemistry Protein Binding Retinaldehyde/metabolism,physiology Rhodopsin/agonists,metabolism Spectrophotometry, Ultraviolet
Chemicals
Rhodopsin GTP-Binding Proteins Retinaldehyde
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Tsukamoto Hisao
Department of Biophysics, Graduate School of Science, Kyoto University and Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Kyoto 606-8502, Japan.
Terakita Akihisa
Shichida Yoshinori
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2005-05-03
Epub
2005-00-25
Pages
6303-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC1088369
Subset
IM
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