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Aminopropyltransferases Involved in Polyamine Biosynthesis Localize Preferentially in the Nucleus of Plant Cells

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Aminopropyltransferases Involved in Polyamine Biosynthesis Localize Preferentially in the Nucleus of Plant Cells

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dc.contributor.author Belda Palazón, Borja es_ES
dc.contributor.author RUIZ, L. es_ES
dc.contributor.author Martí Sanchis, Esmeralda es_ES
dc.contributor.author Tarraga Herrero, Susana es_ES
dc.contributor.author Tiburcio, A. es_ES
dc.contributor.author Culiañez Macia, Francisco Antonio es_ES
dc.contributor.author Farras, R. es_ES
dc.contributor.author Carrasco, P. es_ES
dc.contributor.author Ferrando Monleón, Alejandro Ramón es_ES
dc.date.accessioned 2014-07-16T09:42:33Z
dc.date.available 2014-07-16T09:42:33Z
dc.date.issued 2012-10
dc.identifier.issn 1932-6203
dc.identifier.uri http://hdl.handle.net/10251/38847
dc.description.abstract Plant aminopropyltransferases consist of a group of enzymes that transfer aminopropyl groups derived from decarboxylated S-adenosyl-methionine (dcAdoMet or dcSAM) to propylamine acceptors to produce polyamines, ubiquitous metabolites with positive charge at physiological pH. Spermidine synthase (SPDS) uses putrescine as amino acceptor to form spermidine, whereas spermine synthase (SPMS) and thermospermine synthase (TSPMS) use spermidine as acceptor to synthesize the isomers spermine and thermospermine respectively. In previous work it was shown that both SPDS1 and SPDS2 can physically interact with SPMS although no data concerning the subcellular localization was reported. Here we study the subcellular localization of these enzymes and their protein dimer complexes with gateway-based Bimolecular Fluorescence Complementation (BiFC) binary vectors. In addition, we have characterized the molecular weight of the enzyme complexes by gel filtration chromatography with in vitro assembled recombinant enzymes and with endogenous plant protein extracts. Our data suggest that aminopropyltransferases display a dual subcellular localization both in the cytosol and nuclear enriched fractions, and they assemble preferably as dimers. The BiFC transient expression data suggest that aminopropyltransferase heterodimer complexes take place preferentially inside the nucleus. es_ES
dc.description.sponsorship This work was supported by grants BIO2008-05493-C02-02 and BIO2009-11818 from Spanish Ministerio de Ciencia e Innovacion to A. Ferrando. B. Belda-Palazon is a recipient of a VALi+d predoctoral contract of Generalitat Valenciana ACIF2010/085. The funders had no role in study design, data collection and analysis, decision to publish or preparation of the manuscript. en_EN
dc.language Inglés es_ES
dc.publisher Public Library of Science es_ES
dc.relation info:eu-repo/grantAgreement/MICINN//BIO2008-05493-C02-02/ES/AMINO OXIDASAS Y EXPRESION GENICA/ es_ES
dc.relation info:eu-repo/grantAgreement/MICINN//BIO2009-11818/ES/Hipusinacion Del Factor Eif5A Y Muerte Celular Inducida Por Estres En Plantas/ es_ES
dc.relation VALi+d predoctoral contract of Generalitat Valenciana ACIF2010/085 es_ES
dc.relation.ispartof PLoS ONE es_ES
dc.rights Reconocimiento (by) es_ES
dc.subject Bimolecular fluorescence complementation es_ES
dc.subject Spermidine synthase es_ES
dc.subject Arabidopsis-Thaliana es_ES
dc.subject Protein interactions es_ES
dc.subject Crystal-Structure es_ES
dc.subject S-Adenosylmethionine es_ES
dc.subject Expression es_ES
dc.subject Mechanism es_ES
dc.subject Acyltransferase es_ES
dc.subject Decarboxylase es_ES
dc.title Aminopropyltransferases Involved in Polyamine Biosynthesis Localize Preferentially in the Nucleus of Plant Cells es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1371/journal.pone.0046907
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes es_ES
dc.description.bibliographicCitation Belda Palazón, B.; Ruiz, L.; Martí Sanchis, E.; Tarraga Herrero, S.; Tiburcio, A.; Culiañez Macia, FA.; Farras, R.... (2012). Aminopropyltransferases Involved in Polyamine Biosynthesis Localize Preferentially in the Nucleus of Plant Cells. PLoS ONE. 7:46907-46907. https://doi.org/10.1371/journal.pone.0046907 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://dx.doi.org/10.1371/journal.pone.0046907 es_ES
dc.description.upvformatpinicio 46907 es_ES
dc.description.upvformatpfin 46907 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 7 es_ES
dc.relation.senia 232603
dc.identifier.pmid 23056524 en_EN
dc.identifier.pmcid PMC3466176 en_EN
dc.contributor.funder Ministerio de Ciencia e Innovación es_ES
dc.contributor.funder Ministerio de Ciencia e Innovación es_ES


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