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dc.creatorArroyave C.spa
dc.creatorTolrà R.spa
dc.creatorChaves L.spa
dc.creatorde Souza M.C.spa
dc.creatorBarceló J.spa
dc.creatorPoschenrieder C.spa
dc.date.accessioned2017-12-19T19:36:50Z
dc.date.available2017-12-19T19:36:50Z
dc.date.created2017
dc.identifier.issn1620134spa
dc.identifier.urihttp://hdl.handle.net/11407/4356
dc.description.abstractThe mechanisms of extreme Al-resistance in Urochloa decumbens are not established. Full resistance expression requires a lag time of 72-96h and is preceded by a sensitive phase (24-48h) with Al-induced root growth inhibition. The aim here was to identify key processes of the activation phase of Al-resistance analysing both root exudates and comparative root proteome. Samples were taken after 0, 24 and 96h exposure to 0 or 200μM Al. Al-induced stimulation of citrate and oxalate efflux was limited to the sensitive phase. Only 11 proteins revealed Al-induced abundance differences; six were identified. After 24h, phenylalanine ammonium lyase (PAL), methionine synthase (MS), and deoxymugineic acid synthase (DMAS) decreased, while acid phosphatase (APase) abundance increased. Coincident with growth recovering, PAL and MS, but not DMAS, returned to initial levels. After 96h, γ-carbonic anhydrase (γ-CA) and adenylate kinase (AK) along with two unidentified proteins were more abundant. In conclusion, few protein changes characterize the initial response to Al in signalgrass. During the alarm phase, changes are related to P-mobilization, downregulation of Fe-acquisition, reduction of phenolic biosynthesis, and small stimulation of organic acid exudation. After recovering (resistant phase), biosynthesis of phenolics and methionine, but not Fe-mobilization are re-established. Full expression of Al-resistance is characterized by enhanced γ-CA mediating mitochondrial complex I assembly and increased AK abundance indicating higher root respiration and better provision of ADP and Mg2+ to ATP synthase, respectively. The unidentified proteins and the specific role of γ-CA in Al resistance of U. decumbens will centre future research. © 2017 Elsevier Inc.eng
dc.language.isoengspa
dc.publisherElsevier Inc.spa
dc.relation.isversionofhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85029431673&doi=10.1016%2fj.jinorgbio.2017.09.010&partnerID=40&md5=2c4b9d15d233cbd0db2361c89c233a5dspa
dc.sourceScopusspa
dc.sourcereponame:Repositorio Institucionalspa
dc.sourceinstname:Universidad de Medellínspa
dc.titleA proteomic approach to the mechanisms underlying activation of aluminium resistance in roots of Urochloa decumbensspa
dc.typeArticle in Pressspa
dc.typeinfo:eu-repo/semantics/publishedVersionspa
dc.typeinfo:eu-repo/semantics/otherspa
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccessspa
dc.contributor.affiliationArroyave, C., Plant Physiology Laboratory, Biosciences Faculty, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain, Environmental Engineering Faculty, Universidad de Medellín, 050026 Medellín, Colombiaspa
dc.contributor.affiliationTolrà, R., Plant Physiology Laboratory, Biosciences Faculty, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spainspa
dc.contributor.affiliationChaves, L., Plant Physiology Laboratory, Biosciences Faculty, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spainspa
dc.contributor.affiliationde Souza, M.C., Plant Physiology Laboratory, Biosciences Faculty, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spainspa
dc.contributor.affiliationBarceló, J., Plant Physiology Laboratory, Biosciences Faculty, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spainspa
dc.contributor.affiliationPoschenrieder, C., Plant Physiology Laboratory, Biosciences Faculty, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spainspa
dc.identifier.doi10.1016/j.jinorgbio.2017.09.010spa
dc.subject.keywordAdenylate kinaseeng
dc.subject.keywordAluminium resistanceeng
dc.subject.keywordGamma-carbonic anhydraseeng
dc.subject.keywordOrganic acideng
dc.subject.keywordPhytosiderophoreeng
dc.subject.keywordProteomic changeseng
dc.publisher.facultyFacultad de Ingenieríasspa
dc.abstractThe mechanisms of extreme Al-resistance in Urochloa decumbens are not established. Full resistance expression requires a lag time of 72-96h and is preceded by a sensitive phase (24-48h) with Al-induced root growth inhibition. The aim here was to identify key processes of the activation phase of Al-resistance analysing both root exudates and comparative root proteome. Samples were taken after 0, 24 and 96h exposure to 0 or 200μM Al. Al-induced stimulation of citrate and oxalate efflux was limited to the sensitive phase. Only 11 proteins revealed Al-induced abundance differences; six were identified. After 24h, phenylalanine ammonium lyase (PAL), methionine synthase (MS), and deoxymugineic acid synthase (DMAS) decreased, while acid phosphatase (APase) abundance increased. Coincident with growth recovering, PAL and MS, but not DMAS, returned to initial levels. After 96h, γ-carbonic anhydrase (γ-CA) and adenylate kinase (AK) along with two unidentified proteins were more abundant. In conclusion, few protein changes characterize the initial response to Al in signalgrass. During the alarm phase, changes are related to P-mobilization, downregulation of Fe-acquisition, reduction of phenolic biosynthesis, and small stimulation of organic acid exudation. After recovering (resistant phase), biosynthesis of phenolics and methionine, but not Fe-mobilization are re-established. Full expression of Al-resistance is characterized by enhanced γ-CA mediating mitochondrial complex I assembly and increased AK abundance indicating higher root respiration and better provision of ADP and Mg2+ to ATP synthase, respectively. The unidentified proteins and the specific role of γ-CA in Al resistance of U. decumbens will centre future research. © 2017 Elsevier Inc.eng
dc.creator.affiliationPlant Physiology Laboratory, Biosciences Faculty, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spainspa
dc.creator.affiliationEnvironmental Engineering Faculty, Universidad de Medellín, 050026 Medellín, Colombiaspa
dc.relation.ispartofesJournal of Inorganic Biochemistryspa


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