Salcedo Ernesto, Zheng Lijun, Phistry Meridee, Bagg Eve E, Britt Steven G
Department of Cell and Developmental Biology, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA.
J Neurosci. 2003 Nov 26;23(34):10873-8. doi: 10.1523/JNEUROSCI.23-34-10873.2003.
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.
无脊椎动物对从紫外线到红光的广谱光敏感。紫外线中的颜色敏感性在飞行和陆生无脊椎动物的觅食、导航和配偶选择中起着重要作用。在这里，我们表明单个氨基酸多态性是无脊椎动物紫外线视觉的原因。这个残基（紫外线：赖氨酸与蓝色：天冬酰胺或谷氨酸）对应于牛视紫红质中氨基酸位置甘氨酸90（G90），该位点在常染色体显性人类先天性夜盲中受到影响。在无脊椎动物中引入带正电荷的赖氨酸可能会使席夫碱发色团去质子化并产生紫外线视觉色素。这个相同的位置负责调节几种鸟类的紫外线与蓝色敏感性，这表明紫外线视觉在无脊椎动物和脊椎动物谱系中通过类似的分子机制独立出现。
