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Biochemical quantitation of the eIF5A hypusination in Arabidopsis thaliana uncovers ABA-dependent regulation

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Biochemical quantitation of the eIF5A hypusination in Arabidopsis thaliana uncovers ABA-dependent regulation

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dc.contributor.author Belda Palazón, Borja es_ES
dc.contributor.author Nohales Zafra, Maria Angeles es_ES
dc.contributor.author Rambla Nebot, Jose Luis es_ES
dc.contributor.author Aceña, José L. es_ES
dc.contributor.author Delgado, Oscar es_ES
dc.contributor.author Fustero Lardies, Santos es_ES
dc.contributor.author Martínez, M. Carmen es_ES
dc.contributor.author Granell Richart, Antonio es_ES
dc.contributor.author Carbonell Gisbert, Juan es_ES
dc.contributor.author Ferrando Monleón, Alejandro Ramón es_ES
dc.date.accessioned 2016-07-21T09:23:37Z
dc.date.available 2016-07-21T09:23:37Z
dc.date.issued 2014-05-16
dc.identifier.issn 1664-462X
dc.identifier.uri http://hdl.handle.net/10251/67953
dc.description.abstract The eukaryotic translation elongation factor eIF5A is the only protein known to contain the unusual amino acid hypusine which is essential for its biological activity. This post-translational modification is achieved by the sequential action of the enzymes deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). The crucial molecular function of eIF5A during translation has been recently elucidated in yeast and it is expected to be fully conserved in every eukaryotic cell, however the functional description of this pathway in plants is still sparse. The genetic approaches with transgenic plants for either eIF5A overexpression or antisense have revealed some activities related to the control of cell death processes but the molecular details remain to be characterized. One important aspect of fully understanding this pathway is the biochemical description of the hypusine modification system. Here we have used recombinant eIF5A proteins either modified by hypusination or non-modified to establish a bi-dimensional electrophoresis (2D-E) profile for the three eIF5A protein isoforms and their hypusinated or unmodified proteoforms present in Arabidopsis thaliana. The combined use of the recombinant 2D-E profile together with 2D-E/western blot analysis from whole plant extracts has provided a quantitative approach to measure the hypusination status of eIF5A. We have used this information to demonstrate that treatment with the hormone abscisic acid produces an alteration of the hypusine modification system in Arabidopsis thaliana. Overall this study presents the first biochemical description of the post-translational modification of eIF5A by hypusination which will be functionally relevant for future studies related to the characterization of this pathway in Arabidopsis thaliana. es_ES
dc.language Inglés es_ES
dc.publisher Frontiers Media es_ES
dc.relation.ispartof Frontiers in Plant Science es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject Spermidine es_ES
dc.subject Hypusine es_ES
dc.subject EIF5A es_ES
dc.subject 2D-electrophoresis es_ES
dc.subject Abscisic acid es_ES
dc.title Biochemical quantitation of the eIF5A hypusination in Arabidopsis thaliana uncovers ABA-dependent regulation es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.3389/fpls.2014.00202
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.; Nohales Zafra, MA.; Rambla Nebot, JL.; Aceña, JL.; Delgado, O.; Fustero Lardies, S.; Martínez, MC.... (2014). Biochemical quantitation of the eIF5A hypusination in Arabidopsis thaliana uncovers ABA-dependent regulation. Frontiers in Plant Science. 5:202-1-202-11. doi:10.3389/fpls.2014.00202 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://dx.doi.org/10.3389/fpls.2014.00202 es_ES
dc.description.upvformatpinicio 202-1 es_ES
dc.description.upvformatpfin 202-11 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 5 es_ES
dc.relation.senia 278368 es_ES
dc.identifier.pmcid PMC4032925 en_EN
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