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Commun Biol
2022 Jan 18;51:63. doi: 10.1038/s42003-022-03010-x.
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Amino acid residue at position 188 determines the UV-sensitive bistable property of vertebrate non-visual opsin Opn5.
Fujiyabu C
,
Sato K
,
Nishio Y
,
Imamoto Y
,
Ohuchi H
,
Shichida Y
,
Yamashita T
.
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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.
20K08885 Ministry of Education, Culture, Sports, Science and Technology (MEXT), 19K21848 Ministry of Education, Culture, Sports, Science and Technology (MEXT), 16H02515 Ministry of Education, Culture, Sports, Science and Technology (MEXT), 16K07437 Ministry of Education, Culture, Sports, Science and Technology (MEXT), JPMJCR1753 MEXT | JST | Core Research for Evolutional Science and Technology (CREST)
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