The evolution of protein complexes by duplication of homomeric interactions
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.7/39 |
Resumo: | BACKGROUND: Cellular functions are accomplished by the concerted actions of functional modules. The mechanisms driving the emergence and evolution of these modules are still unclear. Here we investigate the evolutionary origins of protein complexes, modules in physical protein-protein interaction networks. RESULTS: We studied protein complexes in Saccharomyces cerevisiae, complexes of known three-dimensional structure in the Protein Data Bank and clusters of pairwise protein interactions in the networks of several organisms. We found that duplication of homomeric interactions, a large class of protein interactions, frequently results in the formation of complexes of paralogous proteins. This route is a common mechanism for the evolution of complexes and clusters of protein interactions. Our conclusions are further confirmed by theoretical modelling of network evolution. We propose reasons for why this is favourable in terms of structure and function of protein complexes. CONCLUSION: Our study provides the first insight into the evolution of functional modularity in protein-protein interaction networks, and the origins of a large class of protein complexes. |
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The evolution of protein complexes by duplication of homomeric interactionsEvolution, MolecularGene DuplicationModels, GeneticModels, MolecularMultiprotein Complexes/chemistry/*genetics/metabolismProtein Structure, QuaternaryBACKGROUND: Cellular functions are accomplished by the concerted actions of functional modules. The mechanisms driving the emergence and evolution of these modules are still unclear. Here we investigate the evolutionary origins of protein complexes, modules in physical protein-protein interaction networks. RESULTS: We studied protein complexes in Saccharomyces cerevisiae, complexes of known three-dimensional structure in the Protein Data Bank and clusters of pairwise protein interactions in the networks of several organisms. We found that duplication of homomeric interactions, a large class of protein interactions, frequently results in the formation of complexes of paralogous proteins. This route is a common mechanism for the evolution of complexes and clusters of protein interactions. Our conclusions are further confirmed by theoretical modelling of network evolution. We propose reasons for why this is favourable in terms of structure and function of protein complexes. CONCLUSION: Our study provides the first insight into the evolution of functional modularity in protein-protein interaction networks, and the origins of a large class of protein complexes.ARCAPereira Leal, J.B.Levy, E.D.Kamp, C.Teichmann, S.A.2009-09-30T11:44:13Z20072007-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.7/39engPereira-Leal, J. B., Levy, E.D., Kamp, C., Teichmann, S.A. (2007). "Evolution of protein complexes by duplication of homomeric interactions." Genome Biol 8(4): R51.info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2022-11-29T14:34:35Zoai:arca.igc.gulbenkian.pt:10400.7/39Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:11:32.429074Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
The evolution of protein complexes by duplication of homomeric interactions |
title |
The evolution of protein complexes by duplication of homomeric interactions |
spellingShingle |
The evolution of protein complexes by duplication of homomeric interactions Pereira Leal, J.B. Evolution, Molecular Gene Duplication Models, Genetic Models, Molecular Multiprotein Complexes/chemistry/*genetics/metabolism Protein Structure, Quaternary |
title_short |
The evolution of protein complexes by duplication of homomeric interactions |
title_full |
The evolution of protein complexes by duplication of homomeric interactions |
title_fullStr |
The evolution of protein complexes by duplication of homomeric interactions |
title_full_unstemmed |
The evolution of protein complexes by duplication of homomeric interactions |
title_sort |
The evolution of protein complexes by duplication of homomeric interactions |
author |
Pereira Leal, J.B. |
author_facet |
Pereira Leal, J.B. Levy, E.D. Kamp, C. Teichmann, S.A. |
author_role |
author |
author2 |
Levy, E.D. Kamp, C. Teichmann, S.A. |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
ARCA |
dc.contributor.author.fl_str_mv |
Pereira Leal, J.B. Levy, E.D. Kamp, C. Teichmann, S.A. |
dc.subject.por.fl_str_mv |
Evolution, Molecular Gene Duplication Models, Genetic Models, Molecular Multiprotein Complexes/chemistry/*genetics/metabolism Protein Structure, Quaternary |
topic |
Evolution, Molecular Gene Duplication Models, Genetic Models, Molecular Multiprotein Complexes/chemistry/*genetics/metabolism Protein Structure, Quaternary |
description |
BACKGROUND: Cellular functions are accomplished by the concerted actions of functional modules. The mechanisms driving the emergence and evolution of these modules are still unclear. Here we investigate the evolutionary origins of protein complexes, modules in physical protein-protein interaction networks. RESULTS: We studied protein complexes in Saccharomyces cerevisiae, complexes of known three-dimensional structure in the Protein Data Bank and clusters of pairwise protein interactions in the networks of several organisms. We found that duplication of homomeric interactions, a large class of protein interactions, frequently results in the formation of complexes of paralogous proteins. This route is a common mechanism for the evolution of complexes and clusters of protein interactions. Our conclusions are further confirmed by theoretical modelling of network evolution. We propose reasons for why this is favourable in terms of structure and function of protein complexes. CONCLUSION: Our study provides the first insight into the evolution of functional modularity in protein-protein interaction networks, and the origins of a large class of protein complexes. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007 2007-01-01T00:00:00Z 2009-09-30T11:44:13Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.7/39 |
url |
http://hdl.handle.net/10400.7/39 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Pereira-Leal, J. B., Levy, E.D., Kamp, C., Teichmann, S.A. (2007). "Evolution of protein complexes by duplication of homomeric interactions." Genome Biol 8(4): R51. |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799130571373281280 |