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dc.contributor.authorBelda-Palazón, Borja-
dc.contributor.authorNohales, María-Ángeles-
dc.contributor.authorGranell, Antonio-
dc.contributor.authorCarbonell-Gisbert, Juan-
dc.contributor.authorFerrando, Alejandro-
dc.date.accessioned2017-07-14T12:36:46Z-
dc.date.available2017-07-14T12:36:46Z-
dc.date.issued2014-05-16-
dc.identifier.citationFrontiers in Plant Science 5: 202 (2014)-
dc.identifier.issn1664-462X-
dc.identifier.urihttp://hdl.handle.net/10261/153179-
dc.description.abstractThe 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.-
dc.description.sponsorshipWe acknowledge funding from the Spanish MICINN/MINECO (BIO2009-11818 and BIO2011-23828). Borja Belda-Palazón is a recipient of a VALi+d predoctoral (ACIF2010/085) contract of the Generalitat Valenciana.-
dc.publisherFrontiers Media-
dc.relation.isversionofPublisher's version-
dc.rightsopenAccess-
dc.titleBiochemical quantitation of the eIF5A hypusination in Arabidopsis thaliana uncovers ABA-dependent regulation-
dc.typeartículo-
dc.identifier.doi10.3389/fpls.2014.00202-
dc.description.peerreviewedPeer reviewed-
dc.relation.publisherversionhttp://dx.doi.org/10.3389/fpls.2014.00202-
dc.date.updated2017-07-14T12:36:47Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066en-
dc.rights.holderCopyright © 2014 Belda-Palazón, Nohales, Rambla, Aceña, Delgado, Fustero, Martínez, Granell, Carbonell and Ferrando.-
dc.rights.licensehttp://creativecommons.org/licenses/by/4.0/-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.contributor.funderMinisterio de Ciencia e Innovación (España)-
dc.contributor.funderGeneralitat Valenciana-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100004837es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003359es_ES
dc.identifier.pmid24904603-
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