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dc.creatorGutiérrez Beltrán, Emilioes
dc.creatorElander, Pernilla H.es
dc.creatorDalman, Kerstines
dc.creatorDayhoff, Guy W. IIes
dc.creatorMoschou, Panagiotis N.es
dc.creatorUversky, Vladimir N.es
dc.creatorCrespo, José L.es
dc.creatorBozhkov, Peter V.es
dc.date.accessioned2021-09-07T14:05:10Z
dc.date.available2021-09-07T14:05:10Z
dc.date.issued2021
dc.identifier.citationGutiérrez Beltrán, E., Elander, P.H., Dalman, K., Dayhoff, G.W.I., Moschou, P.N., Uversky, V.N.,...,Bozhkov, P.V. (2021). Tudor staphylococcal nuclease is a docking platform for stress granule components and is essential for SnRK1 activation in Arabidopsis. EMBO Journal, 40 (17), e105043.
dc.identifier.issn0261-4189es
dc.identifier.issn1460-2075es
dc.identifier.urihttps://hdl.handle.net/11441/125556
dc.description.abstractTudor staphylococcal nuclease (TSN; also known as Tudor-SN, p100, or SND1) is a multifunctional, evolutionarily conserved regulator of gene expression, exhibiting cytoprotective activity in animals and plants and oncogenic activity in mammals. During stress, TSN stably associates with stress granules (SGs), in a poorly understood process. Here, we show that in the model plant Arabidopsis thaliana, TSN is an intrinsically disordered protein (IDP) acting as a scaffold for a large pool of other IDPs, enriched for conserved stress granule components as well as novel or plant-specific SG-localized proteins. While approximately 30% of TSN interactors are recruited to stress granules de novo upon stress perception, 70% form a protein–protein interaction network present before the onset of stress. Finally, we demonstrate that TSN and stress granule formation promote heat-induced activation of the evolutionarily conserved energy-sensing SNF1-related protein kinase 1 (SnRK1), the plant orthologue of mammalian AMP-activated protein kinase (AMPK). Our results establish TSN as a docking platform for stress granule proteins, with an important role in stress signalling.es
dc.description.sponsorshipEuropean Commission 702473es
dc.description.sponsorshipMinisterio de Economía y Competitividad IJCI-2016-30763, PGC2018-099048-B-100es
dc.description.sponsorshipUniversidad de Sevilla VIPPIT-2020-IV.4, VIPPIT-2020-I.5es
dc.description.sponsorshipKnut and Alice Wallenberg Foundation 2018.0026es
dc.description.sponsorshipSwedish Research Council VR 2019-04250_VRes
dc.description.sponsorshipSwedish Foundation for Strategic Research RBP14-0037es
dc.formatapplication/pdfes
dc.format.extent21 p.es
dc.language.isoenges
dc.publisherWiley-Blackwelles
dc.relation.ispartofEMBO Journal, 40 (17), e105043.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectHeat stresses
dc.subjectIntrinsically disordered regionses
dc.subjectSnRK1/SNF1/AMPKes
dc.subjectStress granuleses
dc.subjectTudor staphylococcal nucleasees
dc.titleTudor staphylococcal nuclease is a docking platform for stress granule components and is essential for SnRK1 activation in Arabidopsises
dc.typeinfo:eu-repo/semantics/articlees
dcterms.identifierhttps://ror.org/03yxnpp24
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.projectID702473es
dc.relation.projectIDIJCI-2016-30763es
dc.relation.projectIDPGC2018-099048-B-100es
dc.relation.projectIDVIPPIT-2020-IV.4es
dc.relation.projectIDVIPPIT-2020-I.5es
dc.relation.projectID2018.0026es
dc.relation.projectID2019-04250_VRes
dc.relation.projectIDRBP14-0037es
dc.relation.publisherversionhttps://doi.org/10.15252/embj.2020105043es
dc.identifier.doi10.15252/embj.2020105043es
dc.journaltitleEMBO Journales
dc.publication.volumen40es
dc.publication.issue17es
dc.publication.initialPagee105043es

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