Department of Biological Sciences, University of Maryland Baltimore County, Baltimore, MD 21250, USA.
Proc Biol Sci. 2012 Jan 7;279(1726):3-14. doi: 10.1098/rspb.2011.1819. Epub 2011 Oct 19.
Opsin proteins are essential molecules in mediating the ability of animals to detect and use light for diverse biological functions. Therefore, understanding the evolutionary history of opsins is key to understanding the evolution of light detection and photoreception in animals. As genomic data have appeared and rapidly expanded in quantity, it has become possible to analyse opsins that functionally and histologically are less well characterized, and thus to examine opsin evolution strictly from a genetic perspective. We have incorporated these new data into a large-scale, genome-based analysis of opsin evolution. We use an extensive phylogeny of currently known opsin sequence diversity as a foundation for examining the evolutionary distributions of key functional features within the opsin clade. This new analysis illustrates the lability of opsin protein-expression patterns, site-specific functionality (i.e. counterion position) and G-protein binding interactions. Further, it demonstrates the limitations of current model organisms, and highlights the need for further characterization of many of the opsin sequence groups with unknown function.
视蛋白是介导动物探测和利用光的多种生物学功能的必需分子。因此,了解视蛋白的进化历史是理解动物光探测和感光进化的关键。随着基因组数据的出现和数量的快速增长,分析功能和组织学上特征不太明显的视蛋白成为可能,从而可以从遗传角度严格研究视蛋白的进化。我们将这些新数据纳入了对视蛋白进化的大规模基于基因组的分析中。我们使用当前已知视蛋白序列多样性的广泛系统发育作为基础,来研究视蛋白进化枝内关键功能特征的进化分布。这项新的分析说明了视蛋白蛋白表达模式、特定位置功能(即反离子位置)和 G 蛋白结合相互作用的不稳定性。此外,它还表明了当前模式生物的局限性,并强调了需要进一步研究许多功能未知的视蛋白序列群。