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dc.creatorGutiérrez Beltrán, Emilioes
dc.creatorPersonat, José Maríaes
dc.creatorTorre, Fernando N. de laes
dc.creatorPozo Cañas, Olga deles
dc.date.accessioned2020-11-04T15:40:05Z
dc.date.available2020-11-04T15:40:05Z
dc.date.issued2017
dc.identifier.citationGutiérrez Beltrán, E., Personat, J.M., Torre, F.N.d.l. y Pozo Cañas, O.d. (2017). A universal stress protein involved in oxidative stress1 is a phosphorylation target for protein kinase CIPK6. Plant Physiology, 173 (1), 836-852.
dc.identifier.issn0032-0889es
dc.identifier.issn1532-2548es
dc.identifier.urihttps://hdl.handle.net/11441/102466
dc.description.abstractCalcineurin B-like interacting protein kinases (CIPKs) decode calcium signals upon interaction with the calcium sensors calcineurin B like proteins into phosphorylation events that result into adaptation to environmental stresses. Few phosphorylation targets of CIPKs are known and therefore the molecular mechanisms underlying their downstream output responses are not fully understood. Tomato (Solanum lycopersicum) Cipk6 regulates immune and susceptible Programmed cell death in immunity transforming Ca2+ signals into reactive oxygen species (ROS) signaling. To investigate SlCipk6-induced molecular mechanisms and identify putative substrates, a yeast two-hybrid approach was carried on and a protein was identified that contained a Universal stress protein (Usp) domain present in bacteria, protozoa and plants, which we named “SlRd2”. SlRd2 was an ATP-binding protein that formed homodimers in planta. SlCipk6 and SlRd2 interacted using coimmunoprecipitation and bimolecular fluorescence complementation (BiFC) assays in Nicotiana benthamiana leaves and the complex localized in the cytosol. SlCipk6 phosphorylated SlRd2 in vitro, thus defining, to our knowledge, a novel target for CIPKs. Heterologous SlRd2 overexpression in yeast conferred resistance to highly toxic LiCl, whereas SlRd2 expression in Escherichia coli UspA mutant restored bacterial viability in response to H2O2 treatment. Finally, transient expression of SlCipk6 in transgenic N. benthamiana SlRd2 overexpressors resulted in reduced ROS accumulation as compared to wild-type plants. Taken together, our results establish that SlRd2, a tomato UspA, is, to our knowledge, a novel interactor and phosphorylation target of a member of the CIPK family, SlCipk6, and functionally regulates SlCipk6-mediated ROS generation.es
dc.description.sponsorshipMinisterio de Economía y Competitividad BIO2005-02136, BIO2009-08648, BIO2013-44750Res
dc.description.sponsorshipJunta de Andalucía P07-CVI-03171es
dc.description.sponsorshipMarie Curie Programme MIRG-CT-2005-031174es
dc.formatapplication/pdfes
dc.format.extent17 p.es
dc.language.isoenges
dc.publisherAmerican Society of Plant Biologistses
dc.relation.ispartofPlant Physiology, 173 (1), 836-852.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleA universal stress protein involved in oxidative stress1 is a phosphorylation target for protein kinase CIPK6es
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Moleculares
dc.relation.projectIDBIO2005-02136es
dc.relation.projectIDBIO2009-08648es
dc.relation.projectIDBIO2013-44750Res
dc.relation.projectIDP07-CVI-03171es
dc.relation.projectIDMIRG-CT-2005-031174es
dc.relation.publisherversionhttps://doi.org/10.1104/pp.16.00949es
dc.identifier.doi10.1104/pp.16.00949es
dc.journaltitlePlant Physiologyes
dc.publication.volumen173es
dc.publication.issue1es
dc.publication.initialPage836es
dc.publication.endPage852es

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