Shedding new light on opsin evolution.
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.
Department of Biological Sciences, University of Maryland Baltimore County, Baltimore, MD 21250, USA. porter@umbc.edu
Megan L
ML
Porter
Joseph R
JR
Blasic
Michael J
MJ
Bok
Evan G
EG
Cameron
Thomas
T
Pringle
Thomas W
TW
Cronin
Phyllis R
PR
Robinson
D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D019143:Evolution, Molecular; D019204:GTP-Binding Proteins / Q000378:metabolism; D007448:Invertebrates / Q000235:genetics* / Q000378:metabolism; D055537:Light Signal Transduction; D055355:Opsins / Q000737:chemistry / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D014714:Vertebrates / Q000235:genetics* / Q000378:metabolism
D000596:Amino Acids; D055355:Opsins; D019204:GTP-Binding Proteins