Shedding new light on opsin evolution
(2012) In Royal Society of London. Proceedings B. Biological Sciences 279(1726). p.3-14- Abstract
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... (More)
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.
(Less)
- author
- Porter, Megan L ; Blasic, Joseph R ; Bok, Michael J LU ; Cameron, Evan G ; Pringle, Thomas ; Cronin, Thomas W and Robinson, Phyllis R
- publishing date
- 2012-01-07
- type
- Contribution to journal
- publication status
- published
- keywords
- Amino Acids/chemistry, Animals, Evolution, Molecular, GTP-Binding Proteins/metabolism, Invertebrates/genetics, Light Signal Transduction, Opsins/chemistry, Phylogeny, Vertebrates/genetics
- in
- Royal Society of London. Proceedings B. Biological Sciences
- volume
- 279
- issue
- 1726
- pages
- 3 - 14
- publisher
- Royal Society Publishing
- external identifiers
-
- scopus:81855224848
- pmid:22012981
- ISSN
- 1471-2954
- DOI
- 10.1098/rspb.2011.1819
- language
- English
- LU publication?
- no
- id
- 649d5a3d-67c3-44ef-9fd4-9583e2c1ce1b
- date added to LUP
- 2020-10-09 10:08:15
- date last changed
- 2024-04-17 18:36:30
@article{649d5a3d-67c3-44ef-9fd4-9583e2c1ce1b,
abstract = {{<p>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.</p>}},
author = {{Porter, Megan L and Blasic, Joseph R and Bok, Michael J and Cameron, Evan G and Pringle, Thomas and Cronin, Thomas W and Robinson, Phyllis R}},
issn = {{1471-2954}},
keywords = {{Amino Acids/chemistry; Animals; Evolution, Molecular; GTP-Binding Proteins/metabolism; Invertebrates/genetics; Light Signal Transduction; Opsins/chemistry; Phylogeny; Vertebrates/genetics}},
language = {{eng}},
month = {{01}},
number = {{1726}},
pages = {{3--14}},
publisher = {{Royal Society Publishing}},
series = {{Royal Society of London. Proceedings B. Biological Sciences}},
title = {{Shedding new light on opsin evolution}},
url = {{http://dx.doi.org/10.1098/rspb.2011.1819}},
doi = {{10.1098/rspb.2011.1819}},
volume = {{279}},
year = {{2012}},
}