Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes
The main object of this study was to investigate the molecular basis for changes in the spectral sensitivity of the visual pigments of deep-sea fishes. The four teleost species studied? Hoplostethus mediterraneus, Cataetyx laticeps, Gonostoma elongatum and Histiobranchus bathybius, are phylogenetica...
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ROYAL SOC LONDON
1997
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ftucl:oai:eprints.ucl.ac.uk.OAI2:123547 2023-05-15T17:35:10+02:00 Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes Hope, AJ Partridge, JC Dulai, KS Hunt, DM 1997-02-22 http://discovery.ucl.ac.uk/123547/ unknown ROYAL SOC LONDON P R SOC B , 264 (1379) 155 - 163. (1997) EASTERN NORTH-ATLANTIC BEARING AMINO-ACIDS BOVINE RHODOPSIN ASSEMBLAGE STRUCTURE VISUAL PIGMENTS FATTY-ACID RED PRESSURE CDNA DETERMINANTS Article 1997 ftucl 2016-01-15T03:02:39Z The main object of this study was to investigate the molecular basis for changes in the spectral sensitivity of the visual pigments of deep-sea fishes. The four teleost species studied? Hoplostethus mediterraneus, Cataetyx laticeps, Gonostoma elongatum and Histiobranchus bathybius, are phylogenetically distant from each other and live at depths ranging from 500 to almost 5000 m. A single fragment of the intronless rod opsin gene was PCR-amplified from each fish and sequenced. The wavelength of peak sensitivity for the rod visual pigments of the four deep-sea species varies from 483 nm in H. mediterraneus and G. elongatum to 468 nm in C. laticeps. Six amino acids at sites on the inner face of the chromophore-binding pocket formed by the seven transmembrane a-helices are identified as candidates for spectral tuning. Substitutions at these sites involve either a change of charge, or a gain or loss of a hydroxyl group. Two of these, at positions 83 and 292, are consistently substituted in the visual pigments of all four species and are likely to be responsible for the shortwave sensitivity of the pigments. Shifts to wavelengths shorter than 480 nm may involve substitution at one or more of the remaining four sites. None of the modifications found in the derived sequences of these opsins suggest functional adaptations, such as increased content of hydroxyl-bearing or proline residues, to resist denaturation by the elevated hydrostatic pressures of the deep sea. Phylogenetic evidence for the duplication of the rod opsin gene in the Anguilliform lineage is presented. Article in Journal/Newspaper North Atlantic University College London: UCL Discovery |
institution |
Open Polar |
collection |
University College London: UCL Discovery |
op_collection_id |
ftucl |
language |
unknown |
topic |
EASTERN NORTH-ATLANTIC BEARING AMINO-ACIDS BOVINE RHODOPSIN ASSEMBLAGE STRUCTURE VISUAL PIGMENTS FATTY-ACID RED PRESSURE CDNA DETERMINANTS |
spellingShingle |
EASTERN NORTH-ATLANTIC BEARING AMINO-ACIDS BOVINE RHODOPSIN ASSEMBLAGE STRUCTURE VISUAL PIGMENTS FATTY-ACID RED PRESSURE CDNA DETERMINANTS Hope, AJ Partridge, JC Dulai, KS Hunt, DM Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes |
topic_facet |
EASTERN NORTH-ATLANTIC BEARING AMINO-ACIDS BOVINE RHODOPSIN ASSEMBLAGE STRUCTURE VISUAL PIGMENTS FATTY-ACID RED PRESSURE CDNA DETERMINANTS |
description |
The main object of this study was to investigate the molecular basis for changes in the spectral sensitivity of the visual pigments of deep-sea fishes. The four teleost species studied? Hoplostethus mediterraneus, Cataetyx laticeps, Gonostoma elongatum and Histiobranchus bathybius, are phylogenetically distant from each other and live at depths ranging from 500 to almost 5000 m. A single fragment of the intronless rod opsin gene was PCR-amplified from each fish and sequenced. The wavelength of peak sensitivity for the rod visual pigments of the four deep-sea species varies from 483 nm in H. mediterraneus and G. elongatum to 468 nm in C. laticeps. Six amino acids at sites on the inner face of the chromophore-binding pocket formed by the seven transmembrane a-helices are identified as candidates for spectral tuning. Substitutions at these sites involve either a change of charge, or a gain or loss of a hydroxyl group. Two of these, at positions 83 and 292, are consistently substituted in the visual pigments of all four species and are likely to be responsible for the shortwave sensitivity of the pigments. Shifts to wavelengths shorter than 480 nm may involve substitution at one or more of the remaining four sites. None of the modifications found in the derived sequences of these opsins suggest functional adaptations, such as increased content of hydroxyl-bearing or proline residues, to resist denaturation by the elevated hydrostatic pressures of the deep sea. Phylogenetic evidence for the duplication of the rod opsin gene in the Anguilliform lineage is presented. |
format |
Article in Journal/Newspaper |
author |
Hope, AJ Partridge, JC Dulai, KS Hunt, DM |
author_facet |
Hope, AJ Partridge, JC Dulai, KS Hunt, DM |
author_sort |
Hope, AJ |
title |
Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes |
title_short |
Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes |
title_full |
Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes |
title_fullStr |
Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes |
title_full_unstemmed |
Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes |
title_sort |
mechanisms of wavelength tuning in the rod opsins of deep-sea fishes |
publisher |
ROYAL SOC LONDON |
publishDate |
1997 |
url |
http://discovery.ucl.ac.uk/123547/ |
genre |
North Atlantic |
genre_facet |
North Atlantic |
op_source |
P R SOC B , 264 (1379) 155 - 163. (1997) |
_version_ |
1766134227524386816 |