TY - JOUR
T1 - Amino acid residue at position 188 determines the UV-sensitive bistable property of vertebrate non-visual opsin Opn5
AU - Fujiyabu, Chihiro
AU - Sato, Keita
AU - Nishio, Yukimi
AU - Imamoto, Yasushi
AU - Ohuchi, Hideyo
AU - Shichida, Yoshinori
AU - Yamashita, Takahiro
N1 - Funding Information:
We thank Dr. E. Nakajima for critical reading of the manuscript. We also thank Prof. R. S. Molday for the generous gift of a Rho1D4-producing hybridoma and Prof. J. Nathans for providing the HEK293S cell line. This work was supported in part by Grants-in-Aid for Scientific Research of MEXT to KS (20K08885), YI (19K21848), YS (16H02515), and TY (16K07437), CREST, JST JPMJCR1753 (TY), a grant from the Kyoto University Foundation (TY), a grant from the Takeda Science Foundation (TY), and a grant from Fujiwara Natural History Foundation (CF).
Publisher Copyright:
© 2022, The Author(s).
PY - 2022/12
Y1 - 2022/12
N2 - 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.
AB - 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.
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U2 - 10.1038/s42003-022-03010-x
DO - 10.1038/s42003-022-03010-x
M3 - Article
C2 - 35042952
AN - SCOPUS:85123120641
SN - 2399-3642
VL - 5
JO - Communications Biology
JF - Communications Biology
IS - 1
M1 - 63
ER -