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In silico characterisation and chromosomal localisation of human RRH (peropsin) – implications for opsin evolution

BACKGROUND: The vertebrate opsins are proteins which utilise a retinaldehyde chromophore in their photosensory or photoisomerase roles in the visual/irradiance detection cycle. The majority of the opsins, such as rod and cone opsins, have a very highly conserved gene structure suggesting a common li...

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Autores principales: Bellingham, James, Wells, Dominic J, Foster, Russell G
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2003
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC149353/
https://www.ncbi.nlm.nih.gov/pubmed/12542842
http://dx.doi.org/10.1186/1471-2164-4-3
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author Bellingham, James
Wells, Dominic J
Foster, Russell G
author_facet Bellingham, James
Wells, Dominic J
Foster, Russell G
author_sort Bellingham, James
collection PubMed
description BACKGROUND: The vertebrate opsins are proteins which utilise a retinaldehyde chromophore in their photosensory or photoisomerase roles in the visual/irradiance detection cycle. The majority of the opsins, such as rod and cone opsins, have a very highly conserved gene structure suggesting a common lineage. Exceptions to this are RGR-opsin and melanopsin, whose genes have very different intron insertion positions. The gene structure of another opsin, peropsin (retinal pigment epithelium-derived rhodopsin homologue, RRH) is unknown. RESULTS: By in silico analysis of the GenBank database we have determined that the human RRH comprises 7 exons spanning approximately 16.5 kb and is localised to chromosome 4q25 in the following gene sequence: cen-EGF-RRH-IF-qter – a position that excludes this gene as a candidate for the RP29 autosomal recessive retinitis pigmentosa locus. A comparison of opsin gene structures reveals that RRH and RGR share two common intron (introns 1 and 4) insertion positions which may reflect a shared ancestral gene. CONCLUSION: The opsins comprise a diverse group of genes which appear to have arisen from three different lineages. These lineages comprise the "classical opsin superfamily" which includes the rod and cone opsins, pinopsin, VA-opsin, parapinopsin and encephalopsin; the RRH and RGR group; and the melanopsin line. A common lineage for RRH and RGR, together with their sites of expression in the RPE, indicates that peropsin may act as a retinal isomerase.
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spelling pubmed-1493532003-02-25 In silico characterisation and chromosomal localisation of human RRH (peropsin) – implications for opsin evolution Bellingham, James Wells, Dominic J Foster, Russell G BMC Genomics Research Article BACKGROUND: The vertebrate opsins are proteins which utilise a retinaldehyde chromophore in their photosensory or photoisomerase roles in the visual/irradiance detection cycle. The majority of the opsins, such as rod and cone opsins, have a very highly conserved gene structure suggesting a common lineage. Exceptions to this are RGR-opsin and melanopsin, whose genes have very different intron insertion positions. The gene structure of another opsin, peropsin (retinal pigment epithelium-derived rhodopsin homologue, RRH) is unknown. RESULTS: By in silico analysis of the GenBank database we have determined that the human RRH comprises 7 exons spanning approximately 16.5 kb and is localised to chromosome 4q25 in the following gene sequence: cen-EGF-RRH-IF-qter – a position that excludes this gene as a candidate for the RP29 autosomal recessive retinitis pigmentosa locus. A comparison of opsin gene structures reveals that RRH and RGR share two common intron (introns 1 and 4) insertion positions which may reflect a shared ancestral gene. CONCLUSION: The opsins comprise a diverse group of genes which appear to have arisen from three different lineages. These lineages comprise the "classical opsin superfamily" which includes the rod and cone opsins, pinopsin, VA-opsin, parapinopsin and encephalopsin; the RRH and RGR group; and the melanopsin line. A common lineage for RRH and RGR, together with their sites of expression in the RPE, indicates that peropsin may act as a retinal isomerase. BioMed Central 2003-01-24 /pmc/articles/PMC149353/ /pubmed/12542842 http://dx.doi.org/10.1186/1471-2164-4-3 Text en Copyright © 2003 Bellingham et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.
spellingShingle Research Article
Bellingham, James
Wells, Dominic J
Foster, Russell G
In silico characterisation and chromosomal localisation of human RRH (peropsin) – implications for opsin evolution
title In silico characterisation and chromosomal localisation of human RRH (peropsin) – implications for opsin evolution
title_full In silico characterisation and chromosomal localisation of human RRH (peropsin) – implications for opsin evolution
title_fullStr In silico characterisation and chromosomal localisation of human RRH (peropsin) – implications for opsin evolution
title_full_unstemmed In silico characterisation and chromosomal localisation of human RRH (peropsin) – implications for opsin evolution
title_short In silico characterisation and chromosomal localisation of human RRH (peropsin) – implications for opsin evolution
title_sort in silico characterisation and chromosomal localisation of human rrh (peropsin) – implications for opsin evolution
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC149353/
https://www.ncbi.nlm.nih.gov/pubmed/12542842
http://dx.doi.org/10.1186/1471-2164-4-3
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