Conserved domains and evolution of secreted phospholipases A2
Autor(a) principal: | |
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Data de Publicação: | 2012 |
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/10400.1/11292 |
Resumo: | Secreted phospholipases A2 (sPLA2s) are lipolytic enzymes present in organisms ranging from prokaryotes to eukaryotes but their origin and emergence are poorly understood. We identified and compared the conserved domains of 333 sPLA2s and proposed a model for their evolution. The conserved domains were grouped into seven categories according to the in silico annotated conserved domain collections of cd00618: PLA2_like and pfam00068: Phospholip_A2_1. PLA2s containing the conserved domain cd04706 (plant-specific PLA2) are present in bacteria and plants. Metazoan PLA2s of the group (G) I/II/V/X PLA2 collection exclusively contain the conserved domain cd00125. GIII PLA2s of both vertebrates and invertebrates contain the conserved domain cd04704 (bee venom-like PLA2), and mammalian GIII PLA2s also contain the conserved domain cd04705 (similar to human GIII PLA2). The sPLA2s of bacteria, fungi and marine invertebrates contain the conserved domain pfam09056 (prokaryotic PLA2) that is the only conserved domain identified in fungal sPLA2s. Pfam06951 (GXII PLA2) is present in bacteria and is widely distributed in eukaryotes. All conserved domains were present across mammalian sPLA2s, with the exception of cd04706 and pfam09056. Notably, no sPLA2s were found in Archaea. Phylogenetic analysis of sPLA2 conserved domains reveals that two main clades, the cd- and the pfam-collection, exist, and that they have evolved via gene-duplication and gene-deletion events. These observations are consistent with the hypothesis that sPLA2s in eukaryotes shared common origins with two types of bacterial sPLA2s, and their persistence during evolution may be related to their role in phospholipid metabolism, which is fundamental for survival. |
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Conserved domains and evolution of secreted phospholipases A2Transition-state analogRice Oryza-SativaCrystal-structureSnake-VenomA(2) EnzymesProteinGenomeCloningClassificationResolutionSecreted phospholipases A2 (sPLA2s) are lipolytic enzymes present in organisms ranging from prokaryotes to eukaryotes but their origin and emergence are poorly understood. We identified and compared the conserved domains of 333 sPLA2s and proposed a model for their evolution. The conserved domains were grouped into seven categories according to the in silico annotated conserved domain collections of cd00618: PLA2_like and pfam00068: Phospholip_A2_1. PLA2s containing the conserved domain cd04706 (plant-specific PLA2) are present in bacteria and plants. Metazoan PLA2s of the group (G) I/II/V/X PLA2 collection exclusively contain the conserved domain cd00125. GIII PLA2s of both vertebrates and invertebrates contain the conserved domain cd04704 (bee venom-like PLA2), and mammalian GIII PLA2s also contain the conserved domain cd04705 (similar to human GIII PLA2). The sPLA2s of bacteria, fungi and marine invertebrates contain the conserved domain pfam09056 (prokaryotic PLA2) that is the only conserved domain identified in fungal sPLA2s. Pfam06951 (GXII PLA2) is present in bacteria and is widely distributed in eukaryotes. All conserved domains were present across mammalian sPLA2s, with the exception of cd04706 and pfam09056. Notably, no sPLA2s were found in Archaea. Phylogenetic analysis of sPLA2 conserved domains reveals that two main clades, the cd- and the pfam-collection, exist, and that they have evolved via gene-duplication and gene-deletion events. These observations are consistent with the hypothesis that sPLA2s in eukaryotes shared common origins with two types of bacterial sPLA2s, and their persistence during evolution may be related to their role in phospholipid metabolism, which is fundamental for survival.Turku University Hospital; Portuguese National Science Foundation (FCT)/CCMARWileySapientiaNevalainen, Timo J.Cardoso, João CRRiikonen, Pentti T.2018-12-07T14:52:58Z2012-022012-02-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/11292eng1742-464X10.1111/j.1742-4658.2011.08453.xinfo: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:RCAAP2023-07-24T10:23:04Zoai:sapientia.ualg.pt:10400.1/11292Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:02:49.102194Repositório 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 |
Conserved domains and evolution of secreted phospholipases A2 |
title |
Conserved domains and evolution of secreted phospholipases A2 |
spellingShingle |
Conserved domains and evolution of secreted phospholipases A2 Nevalainen, Timo J. Transition-state analog Rice Oryza-Sativa Crystal-structure Snake-Venom A(2) Enzymes Protein Genome Cloning Classification Resolution |
title_short |
Conserved domains and evolution of secreted phospholipases A2 |
title_full |
Conserved domains and evolution of secreted phospholipases A2 |
title_fullStr |
Conserved domains and evolution of secreted phospholipases A2 |
title_full_unstemmed |
Conserved domains and evolution of secreted phospholipases A2 |
title_sort |
Conserved domains and evolution of secreted phospholipases A2 |
author |
Nevalainen, Timo J. |
author_facet |
Nevalainen, Timo J. Cardoso, João CR Riikonen, Pentti T. |
author_role |
author |
author2 |
Cardoso, João CR Riikonen, Pentti T. |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Nevalainen, Timo J. Cardoso, João CR Riikonen, Pentti T. |
dc.subject.por.fl_str_mv |
Transition-state analog Rice Oryza-Sativa Crystal-structure Snake-Venom A(2) Enzymes Protein Genome Cloning Classification Resolution |
topic |
Transition-state analog Rice Oryza-Sativa Crystal-structure Snake-Venom A(2) Enzymes Protein Genome Cloning Classification Resolution |
description |
Secreted phospholipases A2 (sPLA2s) are lipolytic enzymes present in organisms ranging from prokaryotes to eukaryotes but their origin and emergence are poorly understood. We identified and compared the conserved domains of 333 sPLA2s and proposed a model for their evolution. The conserved domains were grouped into seven categories according to the in silico annotated conserved domain collections of cd00618: PLA2_like and pfam00068: Phospholip_A2_1. PLA2s containing the conserved domain cd04706 (plant-specific PLA2) are present in bacteria and plants. Metazoan PLA2s of the group (G) I/II/V/X PLA2 collection exclusively contain the conserved domain cd00125. GIII PLA2s of both vertebrates and invertebrates contain the conserved domain cd04704 (bee venom-like PLA2), and mammalian GIII PLA2s also contain the conserved domain cd04705 (similar to human GIII PLA2). The sPLA2s of bacteria, fungi and marine invertebrates contain the conserved domain pfam09056 (prokaryotic PLA2) that is the only conserved domain identified in fungal sPLA2s. Pfam06951 (GXII PLA2) is present in bacteria and is widely distributed in eukaryotes. All conserved domains were present across mammalian sPLA2s, with the exception of cd04706 and pfam09056. Notably, no sPLA2s were found in Archaea. Phylogenetic analysis of sPLA2 conserved domains reveals that two main clades, the cd- and the pfam-collection, exist, and that they have evolved via gene-duplication and gene-deletion events. These observations are consistent with the hypothesis that sPLA2s in eukaryotes shared common origins with two types of bacterial sPLA2s, and their persistence during evolution may be related to their role in phospholipid metabolism, which is fundamental for survival. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-02 2012-02-01T00:00:00Z 2018-12-07T14:52:58Z |
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/10400.1/11292 |
url |
http://hdl.handle.net/10400.1/11292 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1742-464X 10.1111/j.1742-4658.2011.08453.x |
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.publisher.none.fl_str_mv |
Wiley |
publisher.none.fl_str_mv |
Wiley |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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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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