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PLoS One. 2007 Oct 17;2(10):e1054.

The origins of novel protein interactions during animal opsin evolution.

Author information

1
Ecology, Evolution and Marine Biology, University of California at Santa Barbara, Santa Barbara, California, United States of America.

Abstract

BACKGROUND:

Biologists are gaining an increased understanding of the genetic bases of phenotypic change during evolution. Nevertheless, the origins of phenotypes mediated by novel protein-protein interactions remain largely undocumented.

METHODOLOGY/PRINCIPLE FINDINGS:

Here we analyze the evolution of opsin visual pigment proteins from the genomes of early branching animals, including a new class of opsins from Cnidaria. We combine these data with existing knowledge of the molecular basis of opsin function in a rigorous phylogenetic framework. We identify adaptive amino acid substitutions in duplicated opsin genes that correlate with a diversification of physiological pathways mediated by different protein-protein interactions.

CONCLUSIONS/SIGNIFICANCE:

This study documents how gene duplication events early in the history of animals followed by adaptive structural mutations increased organismal complexity by adding novel protein-protein interactions that underlie different physiological pathways. These pathways are central to vision and other photo-reactive phenotypes in most extant animals. Similar evolutionary processes may have been at work in generating other metazoan sensory systems and other physiological processes mediated by signal transduction.

PMID:
17940617
PMCID:
PMC2013938
DOI:
10.1371/journal.pone.0001054
[Indexed for MEDLINE]
Free PMC Article
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