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PMID:14645481
| Citation |
Salcedo, E, Zheng, L, Phistry, M, Bagg, EE and Britt, SG (2003) Molecular basis for ultraviolet vision in invertebrates. J. Neurosci. 23:10873-8 |
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| Abstract |
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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| Keywords |
Amino Acid Substitution; Animals; Animals, Genetically Modified; Cattle; Color Perception/genetics; Color Perception/physiology; Drosophila/genetics; Drosophila/physiology; Drosophila Proteins/chemistry; Drosophila Proteins/genetics; Drosophila Proteins/physiology; Electroretinography; Mutation; Polymorphism, Genetic/genetics; Retinal Pigments/chemistry; Retinal Pigments/genetics; Retinal Pigments/physiology; Rhodopsin/chemistry; Rhodopsin/genetics; Rhodopsin/physiology; Structure-Activity Relationship; Ultraviolet Rays |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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