Molecular basis for ultraviolet vision in invertebrates.
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.
Salcedo
Ernesto
E
Department of Cell and Developmental Biology, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA.
Zheng
Lijun
L
Phistry
Meridee
M
Bagg
Eve E
EE
Britt
Steven G
SG
D019943:Amino Acid Substitution; D000818:Animals; D030801:Animals, Genetically Modified; D002417:Cattle; D003118:Color Perception / Q000235:genetics / Q000502:physiology*; D004330:Drosophila / Q000235:genetics / Q000502:physiology*; D029721:Drosophila Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D004596:Electroretinography; D009154:Mutation; D011110:Polymorphism, Genetic / Q000235:genetics; D012168:Retinal Pigments / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D012243:Rhodopsin / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D013329:Structure-Activity Relationship; D014466:Ultraviolet Rays
D029721:Drosophila Proteins; D012168:Retinal Pigments; D012243:Rhodopsin