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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, Leticia es_ES
dc.contributor.author Martí, Esmeralda es_ES
dc.contributor.author Tárraga, Susana es_ES
dc.contributor.author Tiburcio, Antonio F. es_ES
dc.contributor.author Culiáñez, Francisco es_ES
dc.contributor.author Farrás Rivera, Rosa es_ES
dc.contributor.author Carrasco Sorli, Pedro M. es_ES
dc.contributor.author Ferrando, Alejandro es_ES
dc.date.accessioned 2015-06-19T10:21:23Z
dc.date.available 2015-06-19T10:21:23Z
dc.date.issued 2012 es_ES
dc.identifier.citation PLoS ONE Vol. 7 Issue 10: es_ES
dc.identifier.uri http://hdl.handle.net/10550/44580
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.title Aminopropyltransferases Involved in Polyamine Biosynthesis Localize Preferentially in the Nucleus of Plant Cells es_ES
dc.type journal article es_ES
dc.identifier.doi 10.1371/journal.pone.0046907 es_ES
dc.identifier.idgrec 090061 es_ES

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