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- Title
Amino acid residue at position 188 determines the UV-sensitive bistable property of vertebrate non-visual opsin Opn5.
- Authors
Fujiyabu, Chihiro; Sato, Keita; Nishio, Yukimi; Imamoto, Yasushi; Ohuchi, Hideyo; Shichida, Yoshinori; Yamashita, Takahiro
- Abstract
Opsins are G protein-coupled receptors specialized for photoreception in animals. Opn5 is categorized in an independent opsin group and functions for various non-visual photoreceptions. Among vertebrate Opn5 subgroups (Opn5m, Opn5L1 and Opn5L2), Opn5m and Opn5L2 bind 11-cis retinal to form a UV-sensitive resting state, which is inter-convertible with the all-trans retinal bound active state by photoreception. Thus, these opsins are characterized as bistable opsins. To assess the molecular basis of the UV-sensitive bistable property, we introduced comprehensive mutations at Thr188, which is well conserved among these opsins. The mutations in Opn5m drastically hampered 11-cis retinal incorporation and the bistable photoreaction. Moreover, T188C mutant Opn5m exclusively bound all-trans retinal and thermally self-regenerated to the original form after photoreception, which is similar to the photocyclic property of Opn5L1 bearing Cys188. Therefore, the residue at position 188 underlies the UV-sensitive bistable property of Opn5m and contributes to the diversification of vertebrate Opn5 subgroups. Opn5 functions as a G protein-coupled receptor for photoreception in animals and has UV-sensitive bistable property. The amino acid residue at position 188 is found to be responsible for this property and contributes to the diversification of vertebrate Opn5 subgroups.
- Subjects
AMINO acid residues; G protein coupled receptors; OPSINS; BOUND states; VERTEBRATES
- Publication
Communications Biology, 2022, Vol 5, Issue 1, p1
- ISSN
2399-3642
- Publication type
Article
- DOI
10.1038/s42003-022-03010-x