Conserved domains and evolution of secreted phospholipases A2

Detalhes bibliográficos
Autor(a) principal: Nevalainen, Timo J.
Data de Publicação: 2012
Outros Autores: Cardoso, João CR, Riikonen, Pentti T.
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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spelling 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
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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
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dc.publisher.none.fl_str_mv Wiley
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