Multiple domain insertions and losses in the evolution of the Rab prenylation complex

Detalhes bibliográficos
Autor(a) principal: Rasteiro, R.
Data de Publicação: 2007
Outros Autores: Pereira Leal, J.B.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.7/59
Resumo: BACKGROUND: Rab proteins are regulators of vesicular trafficking, requiring a lipid modification for proper function, prenylation of C-terminal cysteines. This is catalysed by a complex of a catalytic heterodimer (Rab Geranylgeranyl Transferase - RabGGTase) and an accessory protein (Rab Escort Protein. REP). Components of this complex display domain insertions relative to paralogous proteins. The function of these inserted domains is unclear. RESULTS: We profiled the domain architecture of the components of the Rab prenylation complex in evolution. We identified the orthologues of the components of the Rab prenylation machinery in 43 organisms, representing the crown eukaryotic groups. We characterize in detail the domain structure of all these components and the phylogenetic relationships between the individual domains. CONCLUSION: We found different domain insertions in different taxa, in alpha-subunits of RGGTase and REP. Our results suggest that there were multiple insertions, expansions and contractions in the evolution of this prenylation complex
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spelling Multiple domain insertions and losses in the evolution of the Rab prenylation complexProtein PrenylationProtein Structure, Tertiaryrab GTP-Binding Proteins/geneticsGene DuplicationEvolution, MolecularAlkyl and Aryl Transferases/geneticsBACKGROUND: Rab proteins are regulators of vesicular trafficking, requiring a lipid modification for proper function, prenylation of C-terminal cysteines. This is catalysed by a complex of a catalytic heterodimer (Rab Geranylgeranyl Transferase - RabGGTase) and an accessory protein (Rab Escort Protein. REP). Components of this complex display domain insertions relative to paralogous proteins. The function of these inserted domains is unclear. RESULTS: We profiled the domain architecture of the components of the Rab prenylation complex in evolution. We identified the orthologues of the components of the Rab prenylation machinery in 43 organisms, representing the crown eukaryotic groups. We characterize in detail the domain structure of all these components and the phylogenetic relationships between the individual domains. CONCLUSION: We found different domain insertions in different taxa, in alpha-subunits of RGGTase and REP. Our results suggest that there were multiple insertions, expansions and contractions in the evolution of this prenylation complexARCARasteiro, R.Pereira Leal, J.B.2009-10-17T11:35:58Z2007-082007-08-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.7/59engRasteiro, R., Pereira-Leal, J.B. (2007). "Multiple domain insertions and losses in the evolution of the Rab prenylation complex". BMC Evolutionary Biology. 7:1401471-2148info: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:RCAAP2022-11-29T14:34:36Zoai:arca.igc.gulbenkian.pt:10400.7/59Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:11:33.363981Repositório 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 Multiple domain insertions and losses in the evolution of the Rab prenylation complex
title Multiple domain insertions and losses in the evolution of the Rab prenylation complex
spellingShingle Multiple domain insertions and losses in the evolution of the Rab prenylation complex
Rasteiro, R.
Protein Prenylation
Protein Structure, Tertiary
rab GTP-Binding Proteins/genetics
Gene Duplication
Evolution, Molecular
Alkyl and Aryl Transferases/genetics
title_short Multiple domain insertions and losses in the evolution of the Rab prenylation complex
title_full Multiple domain insertions and losses in the evolution of the Rab prenylation complex
title_fullStr Multiple domain insertions and losses in the evolution of the Rab prenylation complex
title_full_unstemmed Multiple domain insertions and losses in the evolution of the Rab prenylation complex
title_sort Multiple domain insertions and losses in the evolution of the Rab prenylation complex
author Rasteiro, R.
author_facet Rasteiro, R.
Pereira Leal, J.B.
author_role author
author2 Pereira Leal, J.B.
author2_role author
dc.contributor.none.fl_str_mv ARCA
dc.contributor.author.fl_str_mv Rasteiro, R.
Pereira Leal, J.B.
dc.subject.por.fl_str_mv Protein Prenylation
Protein Structure, Tertiary
rab GTP-Binding Proteins/genetics
Gene Duplication
Evolution, Molecular
Alkyl and Aryl Transferases/genetics
topic Protein Prenylation
Protein Structure, Tertiary
rab GTP-Binding Proteins/genetics
Gene Duplication
Evolution, Molecular
Alkyl and Aryl Transferases/genetics
description BACKGROUND: Rab proteins are regulators of vesicular trafficking, requiring a lipid modification for proper function, prenylation of C-terminal cysteines. This is catalysed by a complex of a catalytic heterodimer (Rab Geranylgeranyl Transferase - RabGGTase) and an accessory protein (Rab Escort Protein. REP). Components of this complex display domain insertions relative to paralogous proteins. The function of these inserted domains is unclear. RESULTS: We profiled the domain architecture of the components of the Rab prenylation complex in evolution. We identified the orthologues of the components of the Rab prenylation machinery in 43 organisms, representing the crown eukaryotic groups. We characterize in detail the domain structure of all these components and the phylogenetic relationships between the individual domains. CONCLUSION: We found different domain insertions in different taxa, in alpha-subunits of RGGTase and REP. Our results suggest that there were multiple insertions, expansions and contractions in the evolution of this prenylation complex
publishDate 2007
dc.date.none.fl_str_mv 2007-08
2007-08-01T00:00:00Z
2009-10-17T11:35:58Z
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/10400.7/59
url http://hdl.handle.net/10400.7/59
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Rasteiro, R., Pereira-Leal, J.B. (2007). "Multiple domain insertions and losses in the evolution of the Rab prenylation complex". BMC Evolutionary Biology. 7:140
1471-2148
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)
collection 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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