In silico characterisation and chromosomal localisation of human RRH (peropsin) implications for opsin evolution -: art. no. 3

被引:35
作者
Bellingham, J
Wells, DJ
Foster, RG
机构
[1] Charing Cross Hosp, Imperial Coll London, Fac Med,Div Neurosci & Psychol Med, Dept Neuromuscular Dis,Gene Targeting Unit, London W6 8RP, England
[2] Charing Cross Hosp, Imperial Coll London, Fac Med,Div Neurosci & Psychol Med, Dept Integrat & Mol Neurosci, London W6 8RP, England
关键词
D O I
10.1186/1471-2164-4-3
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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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