The amphibian diacylglycerol O-acyltransferase 2 (DGAT2)

dc.contributor.authorSCIANI, JULIANA M.pt_BR
dc.contributor.authorNEVES, ADRIANApt_BR
dc.contributor.authorVASSÃO, RUTH C.pt_BR
dc.contributor.authorSPENCER, PATRICKpt_BR
dc.contributor.authorANTONIAZZI, MARTA M.pt_BR
dc.contributor.authorJARED, CARLOSpt_BR
dc.contributor.authorPIMENTA, DANIEL C.pt_BR
dc.coverageInternacionalpt_BR
dc.date.accessioned2019-08-07T19:01:47Z
dc.date.available2019-08-07T19:01:47Z
dc.date.issued2019pt_BR
dc.description.abstractAmphibians are, currently, considered the first vertebrates that had performed the aquatic to terrestrial transition during evolution; therefore, water balance and dehydration control were prerequisites for such environment conquering. Among anurans, Phyllomedusa is a well-studied genus, due to its peptide-rich skin secretion. Here, we have analyzed the skin secretion of Phyllomedusa distincta targeting the proteins present in the skin secretion. The major soluble protein was chromatographically isolated and utilized to immunize rabbits. Through proteomics approaches, we were able to identify such protein as being the diacylglycerol O-acyltransferase 2 (DGAT2), a crucial enzyme involved in lipid synthesis and in the skin water balance. Immunohistochemistry assays revealed the protein tissular distribution for different animal species, belonging to different branches of the phylogenetic tree. Specifically, there was positivity to the anti-DGAT2 on Amphibians’ skin, and no antibody recognition on fish and mammals’ skins. The DGAT2 multiple sequence alignment reveals some degree of conservation throughout the genera; however, there is a different cysteine pattern among them. Molecular modeling analyses corroborate that the different cysteine pattern leads to distinct 3D structures, explaining the different antibody recognition. Moreover, the protein phylogenetic analyses place the Xenopus DGAT2 (the available amphibian representative) next to the Coelacanthus enzyme, which have led the authors to term this a ‘paleo-protein’. DGAT2 would be, therefore, an ancient protein, crucial to the terrestrial environment conquest, with a unique folding—as indicated by the molecular models and immunohistochemistry analyses—a consequence of the different cysteine pattern but with conserved biological function.pt_BR
dc.description.sponsorshipFinanciadora de Estudos e Projetos (FINEP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipIDFINEP: 01.09.0278.04; 01.12.0450.03pt_BR
dc.description.sponsorshipIDCNPq: 303792/2016-7pt_BR
dc.format.extent83-94pt_BR
dc.identifier.citationSCIANI, JULIANA M.; NEVES, ADRIANA; VASSÃO, RUTH C.; SPENCER, PATRICK; ANTONIAZZI, MARTA M.; JARED, CARLOS; PIMENTA, DANIEL C. The amphibian diacylglycerol O-acyltransferase 2 (DGAT2): a ‘paleoprotein’ with conserved function but unique folding. <b>Protein Journal</b>, v. 38, n. 1, p. 83-94, 2019. DOI: <a href="https://dx.doi.org/10.1007/s10930-019-09814-x">10.1007/s10930-019-09814-x</a>. Disponível em: http://repositorio.ipen.br/handle/123456789/30037.
dc.identifier.doi10.1007/s10930-019-09814-xpt_BR
dc.identifier.fasciculo1pt_BR
dc.identifier.issn1572-3887pt_BR
dc.identifier.orcid0000-0001-8949-7735pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-8949-7735
dc.identifier.percentilfi10.269pt_BR
dc.identifier.percentilfiCiteScore30.25
dc.identifier.urihttp://repositorio.ipen.br/handle/123456789/30037
dc.identifier.vol38pt_BR
dc.relation.ispartofProtein Journalpt_BR
dc.rightsopenAccesspt_BR
dc.subjectamphibians
dc.subjectpeptides
dc.subjectskin
dc.subjectproteins
dc.subjectsecretion
dc.subjectchemical analysis
dc.subjecttemperature control
dc.titleThe amphibian diacylglycerol O-acyltransferase 2 (DGAT2)pt_BR
dc.typeArtigo de periódicopt_BR
dspace.entity.typePublication
ipen.autorPATRICK JACK SPENCER
ipen.codigoautor910
ipen.contributor.ipenauthorPATRICK JACK SPENCER
ipen.date.recebimento19-08
ipen.identifier.fi1.317pt_BR
ipen.identifier.fiCiteScore2.0
ipen.identifier.ipendoc25830pt_BR
ipen.identifier.iwosWoSpt_BR
ipen.range.fi0.001 - 1.499
ipen.range.percentilfi0.00 - 24.99
ipen.subtituloa ‘paleoprotein’ with conserved function but unique foldingpt_BR
ipen.type.genreArtigo
relation.isAuthorOfPublication4eb7939e-aeea-4991-8525-b3d05ac27364
relation.isAuthorOfPublication.latestForDiscovery4eb7939e-aeea-4991-8525-b3d05ac27364
sigepi.autor.atividadeSPENCER, PATRICK:910:820:Npt_BR
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