| Molecular basis for ultraviolet vision in invertebrates. | |
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MedLine Citation:
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PMID: 14645481 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Invertebrates are sensitive to a broad spectrum of light that ranges from UV to red. Color sensitivity in the UV plays an important role in foraging, navigation, and mate selection in both flying and terrestrial invertebrate animals. Here, we show that a single amino acid polymorphism is responsible for invertebrate UV vision. This residue (UV: lysine vs blue:asparagine or glutamate) corresponds to amino acid position glycine 90 (G90) in bovine rhodopsin, a site affected in autosomal dominant human congenital night blindness. Introduction of the positively charged lysine in invertebrates is likely to deprotonate the Schiff base chromophore and produce an UV visual pigment. This same position is responsible for regulating UV versus blue sensitivity in several bird species, suggesting that UV vision has arisen independently in invertebrate and vertebrate lineages by a similar molecular mechanism. |
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Authors:
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Ernesto Salcedo; Lijun Zheng; Meridee Phistry; Eve E Bagg; Steven G Britt |
Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of neuroscience : the official journal of the Society for Neuroscience Volume: 23 ISSN: 1529-2401 ISO Abbreviation: J. Neurosci. Publication Date: 2003 Nov |
Date Detail:
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Created Date: 2003-12-03 Completed Date: 2003-12-16 Revised Date: 2010-09-20 |
Medline Journal Info:
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Nlm Unique ID: 8102140 Medline TA: J Neurosci Country: United States |
Other Details:
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Languages: eng Pagination: 10873-8 Citation Subset: IM |
Affiliation:
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Department of Cell and Developmental Biology, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Substitution Animals Animals, Genetically Modified Cattle Color Perception / genetics, physiology* Drosophila / genetics, physiology* Drosophila Proteins / chemistry, genetics, physiology Electroretinography Mutation Polymorphism, Genetic / genetics Retinal Pigments / chemistry, genetics, physiology Rhodopsin / chemistry, genetics, physiology Structure-Activity Relationship Ultraviolet Rays* |
| Grant Support | |
ID/Acronym/Agency:
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R01 EY010759-09/EY/NEI NIH HHS; R01-EY10759/EY/NEI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Drosophila Proteins; 0/Retinal Pigments; 9009-81-8/Rhodopsin |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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