Cargando…

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

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 rho...

Descripción completa

Detalles Bibliográficos
Autores principales: Sakata, Rie, Kabutomori, Ryo, Okano, Keiko, Mitsui, Hiromasa, Takemura, Akihiro, Miwa, Tetsuya, Yamamoto, Hiroyuki, Okano, Toshiyuki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4537116/
https://www.ncbi.nlm.nih.gov/pubmed/26275172
http://dx.doi.org/10.1371/journal.pone.0135888
_version_ 1782385851001470976
author Sakata, Rie
Kabutomori, Ryo
Okano, Keiko
Mitsui, Hiromasa
Takemura, Akihiro
Miwa, Tetsuya
Yamamoto, Hiroyuki
Okano, Toshiyuki
author_facet Sakata, Rie
Kabutomori, Ryo
Okano, Keiko
Mitsui, Hiromasa
Takemura, Akihiro
Miwa, Tetsuya
Yamamoto, Hiroyuki
Okano, Toshiyuki
author_sort Sakata, Rie
collection PubMed
description 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.
format Online
Article
Text
id pubmed-4537116
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-45371162015-08-20 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 PLoS One Research Article 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. Public Library of Science 2015-08-14 /pmc/articles/PMC4537116/ /pubmed/26275172 http://dx.doi.org/10.1371/journal.pone.0135888 Text en © 2015 Sakata et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
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
title Rhodopsin in the Dark Hot Sea: Molecular Analysis of Rhodopsin in a Snailfish, Careproctus rhodomelas, Living near the Deep-Sea Hydrothermal Vent
title_full Rhodopsin in the Dark Hot Sea: Molecular Analysis of Rhodopsin in a Snailfish, Careproctus rhodomelas, Living near the Deep-Sea Hydrothermal Vent
title_fullStr Rhodopsin in the Dark Hot Sea: Molecular Analysis of Rhodopsin in a Snailfish, Careproctus rhodomelas, Living near the Deep-Sea Hydrothermal Vent
title_full_unstemmed Rhodopsin in the Dark Hot Sea: Molecular Analysis of Rhodopsin in a Snailfish, Careproctus rhodomelas, Living near the Deep-Sea Hydrothermal Vent
title_short Rhodopsin in the Dark Hot Sea: Molecular Analysis of Rhodopsin in a Snailfish, Careproctus rhodomelas, Living near the Deep-Sea Hydrothermal Vent
title_sort rhodopsin in the dark hot sea: molecular analysis of rhodopsin in a snailfish, careproctus rhodomelas, living near the deep-sea hydrothermal vent
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4537116/
https://www.ncbi.nlm.nih.gov/pubmed/26275172
http://dx.doi.org/10.1371/journal.pone.0135888
work_keys_str_mv AT sakatarie rhodopsininthedarkhotseamolecularanalysisofrhodopsininasnailfishcareproctusrhodomelaslivingnearthedeepseahydrothermalvent
AT kabutomoriryo rhodopsininthedarkhotseamolecularanalysisofrhodopsininasnailfishcareproctusrhodomelaslivingnearthedeepseahydrothermalvent
AT okanokeiko rhodopsininthedarkhotseamolecularanalysisofrhodopsininasnailfishcareproctusrhodomelaslivingnearthedeepseahydrothermalvent
AT mitsuihiromasa rhodopsininthedarkhotseamolecularanalysisofrhodopsininasnailfishcareproctusrhodomelaslivingnearthedeepseahydrothermalvent
AT takemuraakihiro rhodopsininthedarkhotseamolecularanalysisofrhodopsininasnailfishcareproctusrhodomelaslivingnearthedeepseahydrothermalvent
AT miwatetsuya rhodopsininthedarkhotseamolecularanalysisofrhodopsininasnailfishcareproctusrhodomelaslivingnearthedeepseahydrothermalvent
AT yamamotohiroyuki rhodopsininthedarkhotseamolecularanalysisofrhodopsininasnailfishcareproctusrhodomelaslivingnearthedeepseahydrothermalvent
AT okanotoshiyuki rhodopsininthedarkhotseamolecularanalysisofrhodopsininasnailfishcareproctusrhodomelaslivingnearthedeepseahydrothermalvent