Rhodopsin in the dark hot sea

Molecular analysis of rhodopsin in a snailfish, Careproctus rhodomelas, living near the deep-sea hydrothermal vent

Rie Sakata, Ryo Kabutomori, Keiko Okano, Hiromasa Mitsui, Akihiro Takemura, Tetsuya Miwa, Hiroyuki Yamamoto, Toshiyuki Okano

    Research output: Contribution to journalArticle

    1 Citation (Scopus)

    Abstract

    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 (λmax) 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 A1- 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.

    Original languageEnglish
    Article number0135888
    JournalPLoS One
    Volume10
    Issue number8
    DOIs
    Publication statusPublished - 2015 Aug 14

    Fingerprint

    Hydrothermal Vents
    rhodopsin
    Rhodopsin
    Vents
    Oceans and Seas
    marine fish
    Fish
    Retinaldehyde
    Fishes
    Spectroscopic analysis
    Eye Proteins
    Complementary DNA
    pigments
    Bioluminescence
    Retinal Pigments
    bioluminescence
    Food Supply
    proteins
    Chromophores
    blue light

    ASJC Scopus subject areas

    • Agricultural and Biological Sciences(all)
    • Biochemistry, Genetics and Molecular Biology(all)
    • Medicine(all)

    Cite this

    Rhodopsin in the dark hot sea : Molecular analysis of rhodopsin in a snailfish, Careproctus rhodomelas, living near the deep-sea hydrothermal vent. / Sakata, Rie; Kabutomori, Ryo; Okano, Keiko; Mitsui, Hiromasa; Takemura, Akihiro; Miwa, Tetsuya; Yamamoto, Hiroyuki; Okano, Toshiyuki.

    In: PLoS One, Vol. 10, No. 8, 0135888, 14.08.2015.

    Research output: Contribution to journalArticle

    Sakata, Rie ; Kabutomori, Ryo ; Okano, Keiko ; Mitsui, Hiromasa ; Takemura, Akihiro ; Miwa, Tetsuya ; Yamamoto, Hiroyuki ; Okano, Toshiyuki. / Rhodopsin in the dark hot sea : Molecular analysis of rhodopsin in a snailfish, Careproctus rhodomelas, living near the deep-sea hydrothermal vent. In: PLoS One. 2015 ; Vol. 10, No. 8.
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    abstract = "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 (λmax) 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 A1- 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.",
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