Animals use light information not only for vision but for non-visual functions, such as circadian entrainment and pupillary light response. Opsins, underling molecules of these photoreceptions, are diversified. We aimed to reveal relationships between the diversity of opsins and that of photoreceptive systems by biochemical and spectroscopic analyses of varied opsins. We cloned seven opsins from amphioxus (
Branchiostoma belcheri) and succeeded in functional expression of amphioxus homologues of the Go-coupled opsin and the perospin, whose molecular properties have been largely unknown, in HEK293 cells. Spectroscopic analyses revealed that the Go-coupled opsin and the peropsin bind 11-cis and all-trans retinals, respectively as a chromophore. The results strongly suggest that the physiological function of peropsin is a retinal photoisomerase, while 11-cis configuration is necessary for the Go-coupled opsin. We also demonstrated that the amphioxus homologue of melanopsin, which functions as the circadian photopigment in the photosensitive retinal ganglion cells in mammals, is considerably similar to invertebrate visual pigments in biochemical and photochemical properties for the first time. This finding suggested the evolutionary linkage between invertebrate rhabdomeric visual cells and vertebrate photosensitive retinal ganglion cells. We also showed that the parapinopsin is the UV pigment in the lamprey (
Lethenteron japonica) pineal and is the bistable pigment having photointerconvertible two stable states, that is, the original and the G-protein-activating states. The bistable nature of the parapinopsin can account for the photorecovery of the pineal UV-sensitivity by background green light. Our approach could provide cues to understand the evolution of physiological functions.
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