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Visual systems in deep-sea fishes have been previously studied from a photobiological aspect; however, those of deep-sea fish inhabiting the hydrothermal vents are far less understood due to sampling difficulties. In this study, we analyzed the visual pigment of a deep-sea snailfish,  Careproctus rhodomelas , discovered and collected only near the hydrothermal vents of oceans around Japan. Proteins were solubilized from the  C .  rhodomelas  eyeball and subjected to spectroscopic analysis, which revealed the presence of a pigment characterized by an absorption maximum (λ max ) at 480 nm. Immunoblot analysis of the ocular protein showed a rhodopsin-like immunoreactivity. We also isolated a retinal cDNA encoding the entire coding sequence of putative  C .  rhodomelas  rhodopsin (CrRh). HEK293EBNA cells were transfected with the CrRh cDNA and the proteins extracted from the cells were subjected to spectroscopic analysis. The recombinant CrRh showed the absorption maximum at 480 nm in the presence of 11- cis  retinal. Comparison of the results from the eyeball extract and the recombinant CrRh strongly suggests that CrRh has an A 1 -based 11- cis -retinal chromophore and works as a photoreceptor in the  C .  rhodomelas  retina, and hence that  C .  rhodomelas  responds to dim blue light much the same as other deep-sea fishes. Because hydrothermal vent is a huge supply of viable food,  C .  rhodomelas  likely do not need to participate diel vertical migration and may recognize the bioluminescence produced by aquatic animals living near the hydrothermal vents.

Rhodopsin in the Dark Hot Sea: Molecular Analysis of Rhodopsin in a Snailfish, Careproctus rhodomelas, Living near the Deep-Sea Hydrothermal Vent