Repository logo
 
Publication

Conserved domains and evolution of secreted phospholipases A2

2012-02Journal article Open Access
Simple item page
dc.contributor.authorNevalainen, Timo J.
dc.contributor.authorCardoso, João CR
dc.contributor.authorRiikonen, Pentti T.
dc.date.accessioned2018-12-07T14:52:58Z
dc.date.available2018-12-07T14:52:58Z
dc.date.issued2012-02
dc.description.abstractSecreted 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.
dc.description.sponsorshipTurku University Hospital; Portuguese National Science Foundation (FCT)/CCMAR
dc.description.versioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doi10.1111/j.1742-4658.2011.08453.x
dc.identifier.issn1742-464X
dc.identifier.issn1742-4658
dc.identifier.urihttp://hdl.handle.net/10400.1/11292
dc.language.isoeng
dc.peerreviewedyes
dc.publisherWiley
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectTransition-state analog
dc.subjectRice Oryza-Sativa
dc.subjectCrystal-structure
dc.subjectSnake-Venom
dc.subjectA(2) Enzymes
dc.subjectProtein
dc.subjectGenome
dc.subjectCloning
dc.subjectClassification
dc.subjectResolution
dc.titleConserved domains and evolution of secreted phospholipases A2
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage649
oaire.citation.issue4
oaire.citation.startPage636
oaire.citation.titleFEBS Journal
oaire.citation.volume279
person.familyNameCardoso
person.givenNameJoão
person.identifier14332
person.identifier.ciencia-id8B16-F203-2AFC
person.identifier.orcid0000-0001-7890-0170
person.identifier.ridM-4151-2013
person.identifier.scopus-author-id7201822956
rcaap.rightsopenAccess
rcaap.typearticle
relation.isAuthorOfPublication1b670c84-15e3-4776-8871-50f9eb0eed0d
relation.isAuthorOfPublication.latestForDiscovery1b670c84-15e3-4776-8871-50f9eb0eed0d

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
H11292.pdf
Size:
1.45 MB
Format:
Adobe Portable Document Format
Download

Collections

CCM2-Artigos (em revistas ou actas indexadas)