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dc.contributor.authorPayá-Milans, Miriames_ES
dc.contributor.authorAznar-Moreno, José A.es_ES
dc.contributor.authorBalbuena, Tiago S.es_ES
dc.contributor.authorHaslam, Richard P.es_ES
dc.contributor.authorGidda, Satinder K.es_ES
dc.contributor.authorPérez-Hormaeche, J.es_ES
dc.contributor.authorMullen, Robert T.es_ES
dc.contributor.authorThelen, Jay J.es_ES
dc.contributor.authorNapier, Johnathan A.es_ES
dc.contributor.authorSalas, Joaquín J.es_ES
dc.contributor.authorGarcés Mancheño, Rafaeles_ES
dc.contributor.authorMartínez-Force, Enriquees_ES
dc.contributor.authorVenegas-Calerón, Mónicaes_ES
dc.date.accessioned2016-10-26T10:56:30Z-
dc.date.available2016-10-26T10:56:30Z-
dc.date.issued2016-11-
dc.identifier.citationPlant Science 252: 42–52 (2016)es_ES
dc.identifier.issn0168-9452-
dc.identifier.urihttp://hdl.handle.net/10261/139381-
dc.description62 Páginas; 7 Figuras; 3 Tablases_ES
dc.description.abstractIn oil crops, triacylglycerol biosynthesis is an important metabolic pathway in which glycerol-3-phosphate acyltransferase (GPAT) performs the first acylation step. Mass spectrometry analysis of developing sunflower (Helianthus annuus) seed membrane fractions identified an abundant GPAT, HaGPAT9 isoform 1, with a N-terminal peptide that possessed two phosphorylated residues with possible regulatory function. HaGPAT9-1 belongs to a broad eukaryotic GPAT family, similar to mammalian GPAT3, and it represents one of the two sunflower GPAT9 isoforms, sharing 90% identity with HaGPAT9-2. Both sunflower genes are expressed during seed development and in vegetative tissues, with HaGPAT9-1 transcripts accumulating at relatively higher levels than those for HaGPAT9-2. Green fluorescent protein tagging of HaGPAT9-1 confirmed its subcellular accumulation in the endoplasmic reticulum. Despite their overall sequence similarities, the two sunflower isoforms displayed significant differences in their enzymatic activities. For instance, HaGPAT9-1 possesses in vivo GPAT activity that rescues the lethal phenotype of the cmy228 yeast strain, while in vitro assays revealed a preference of HaGPAT9-1 for palmitoyl-, oleoyl- and linoleoyl-CoAs of one order of magnitude, with the highest increase in yield for oleoyl- and linoleoyl-CoAs. By contrast, no enzymatic activity could be detected for HaGPAT9-2, even though its over-expression modified the TAG profile of yeast.es_ES
dc.description.sponsorshipThis work was supported by the “Ministerio de Economia y Competitividad” and FEDER [AGL2014-53537-R and JAE-CSIC to M.P-M].es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.relationMINECO/ICTI2013-2016/AGL2014-53537-Res_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectEndoplasmic reticulumes_ES
dc.subjectGlycerol-3-phosphate acyltransferasees_ES
dc.subjectHelianthus annuuses_ES
dc.subjectMass spectrometryes_ES
dc.subjectTriacylglyceroles_ES
dc.subjectYeastes_ES
dc.titleSunflower HaGPAT9-1 is the predominant GPAT during seed developmentes_ES
dc.typeArtículoes_ES
dc.identifier.doi10.1016/j.plantsci.2016.07.002-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.plantsci.2016.07.002es_ES
dc.identifier.e-issn1873-2259-
dc.embargo.terms2018-11-01es_ES
dc.rights.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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