The origins of novel protein interactions during animal opsin evolution.
<h4>Background</h4>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.<h4>Methodology/principle findings<...
Guardado en:
Autores principales: | , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2007
|
Materias: | |
Acceso en línea: | https://doaj.org/article/92cd2a4c11674c67acde5e05d5f38c24 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:92cd2a4c11674c67acde5e05d5f38c24 |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:92cd2a4c11674c67acde5e05d5f38c242021-11-25T06:10:40ZThe origins of novel protein interactions during animal opsin evolution.1932-620310.1371/journal.pone.0001054https://doaj.org/article/92cd2a4c11674c67acde5e05d5f38c242007-10-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0001054https://doaj.org/toc/1932-6203<h4>Background</h4>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.<h4>Methodology/principle findings</h4>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.<h4>Conclusions/significance</h4>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.David C PlachetzkiBernard M DegnanTodd H OakleyPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 2, Iss 10, p e1054 (2007) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Medicine R Science Q |
spellingShingle |
Medicine R Science Q David C Plachetzki Bernard M Degnan Todd H Oakley The origins of novel protein interactions during animal opsin evolution. |
description |
<h4>Background</h4>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.<h4>Methodology/principle findings</h4>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.<h4>Conclusions/significance</h4>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. |
format |
article |
author |
David C Plachetzki Bernard M Degnan Todd H Oakley |
author_facet |
David C Plachetzki Bernard M Degnan Todd H Oakley |
author_sort |
David C Plachetzki |
title |
The origins of novel protein interactions during animal opsin evolution. |
title_short |
The origins of novel protein interactions during animal opsin evolution. |
title_full |
The origins of novel protein interactions during animal opsin evolution. |
title_fullStr |
The origins of novel protein interactions during animal opsin evolution. |
title_full_unstemmed |
The origins of novel protein interactions during animal opsin evolution. |
title_sort |
origins of novel protein interactions during animal opsin evolution. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2007 |
url |
https://doaj.org/article/92cd2a4c11674c67acde5e05d5f38c24 |
work_keys_str_mv |
AT davidcplachetzki theoriginsofnovelproteininteractionsduringanimalopsinevolution AT bernardmdegnan theoriginsofnovelproteininteractionsduringanimalopsinevolution AT toddhoakley theoriginsofnovelproteininteractionsduringanimalopsinevolution AT davidcplachetzki originsofnovelproteininteractionsduringanimalopsinevolution AT bernardmdegnan originsofnovelproteininteractionsduringanimalopsinevolution AT toddhoakley originsofnovelproteininteractionsduringanimalopsinevolution |
_version_ |
1718414115479748608 |