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Evolutionary history and functional implications of protein domains and their combinations in eukaryotes

BACKGROUND: In higher multicellular eukaryotes, complex protein domain combinations contribute to various cellular functions such as regulation of intercellular or intracellular signaling and interactions. To elucidate the characteristics and evolutionary mechanisms that underlie such domain combina...

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Autores principales: Itoh, Masumi, Nacher, Jose C, Kuma, Kei-ichi, Goto, Susumu, Kanehisa, Minoru
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2394772/
https://www.ncbi.nlm.nih.gov/pubmed/17588271
http://dx.doi.org/10.1186/gb-2007-8-6-r121
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author Itoh, Masumi
Nacher, Jose C
Kuma, Kei-ichi
Goto, Susumu
Kanehisa, Minoru
author_facet Itoh, Masumi
Nacher, Jose C
Kuma, Kei-ichi
Goto, Susumu
Kanehisa, Minoru
author_sort Itoh, Masumi
collection PubMed
description BACKGROUND: In higher multicellular eukaryotes, complex protein domain combinations contribute to various cellular functions such as regulation of intercellular or intracellular signaling and interactions. To elucidate the characteristics and evolutionary mechanisms that underlie such domain combinations, it is essential to examine the different types of domains and their combinations among different groups of eukaryotes. RESULTS: We observed a large number of group-specific domain combinations in animals, especially in vertebrates. Examples include animal-specific combinations in tyrosine phosphorylation systems and vertebrate-specific combinations in complement and coagulation cascades. These systems apparently underwent extensive evolution in the ancestors of these groups. In extant animals, especially in vertebrates, animal-specific domains have greater connectivity than do other domains on average, and contribute to the varying number of combinations in each animal subgroup. In other groups, the connectivities of older domains were greater on average. To observe the global behavior of domain combinations during evolution, we traced the changes in domain combinations among animals and fungi in a network analysis. Our results indicate that there is a correlation between the differences in domain combinations among different phylogenetic groups and different global behaviors. CONCLUSION: Rapid emergence of animal-specific domains was observed in animals, contributing to specific domain combinations and functional diversification, but no such trends were observed in other clades of eukaryotes. We therefore suggest that the strategy for achieving complex multicellular systems in animals differs from that of other eukaryotes.
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spelling pubmed-23947722008-05-29 Evolutionary history and functional implications of protein domains and their combinations in eukaryotes Itoh, Masumi Nacher, Jose C Kuma, Kei-ichi Goto, Susumu Kanehisa, Minoru Genome Biol Research BACKGROUND: In higher multicellular eukaryotes, complex protein domain combinations contribute to various cellular functions such as regulation of intercellular or intracellular signaling and interactions. To elucidate the characteristics and evolutionary mechanisms that underlie such domain combinations, it is essential to examine the different types of domains and their combinations among different groups of eukaryotes. RESULTS: We observed a large number of group-specific domain combinations in animals, especially in vertebrates. Examples include animal-specific combinations in tyrosine phosphorylation systems and vertebrate-specific combinations in complement and coagulation cascades. These systems apparently underwent extensive evolution in the ancestors of these groups. In extant animals, especially in vertebrates, animal-specific domains have greater connectivity than do other domains on average, and contribute to the varying number of combinations in each animal subgroup. In other groups, the connectivities of older domains were greater on average. To observe the global behavior of domain combinations during evolution, we traced the changes in domain combinations among animals and fungi in a network analysis. Our results indicate that there is a correlation between the differences in domain combinations among different phylogenetic groups and different global behaviors. CONCLUSION: Rapid emergence of animal-specific domains was observed in animals, contributing to specific domain combinations and functional diversification, but no such trends were observed in other clades of eukaryotes. We therefore suggest that the strategy for achieving complex multicellular systems in animals differs from that of other eukaryotes. BioMed Central 2007 2007-06-25 /pmc/articles/PMC2394772/ /pubmed/17588271 http://dx.doi.org/10.1186/gb-2007-8-6-r121 Text en Copyright © 2007 Itoh et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Itoh, Masumi
Nacher, Jose C
Kuma, Kei-ichi
Goto, Susumu
Kanehisa, Minoru
Evolutionary history and functional implications of protein domains and their combinations in eukaryotes
title Evolutionary history and functional implications of protein domains and their combinations in eukaryotes
title_full Evolutionary history and functional implications of protein domains and their combinations in eukaryotes
title_fullStr Evolutionary history and functional implications of protein domains and their combinations in eukaryotes
title_full_unstemmed Evolutionary history and functional implications of protein domains and their combinations in eukaryotes
title_short Evolutionary history and functional implications of protein domains and their combinations in eukaryotes
title_sort evolutionary history and functional implications of protein domains and their combinations in eukaryotes
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2394772/
https://www.ncbi.nlm.nih.gov/pubmed/17588271
http://dx.doi.org/10.1186/gb-2007-8-6-r121
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