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dc.creatorGonzález Arzola, Katiuskaes
dc.creatorDíaz Quintana, Antonio Jesúses
dc.creatorRivero Rodríguez, Franciscoes
dc.creatorVelázquez Campoy, Adriánes
dc.creatorRosa Acosta, Miguel Ángel de laes
dc.creatorDíaz Moreno, Irenees
dc.date.accessioned2017-08-30T17:01:24Z
dc.date.available2017-08-30T17:01:24Z
dc.date.issued2017
dc.identifier.citationGonzález Arzola, K., Díaz Quintana, A., Rivero Rodríguez, F., Velázquez Campoy, A., Rosa, M.A.d.l. y Díaz Moreno, I. (2017). Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c. Nucleic Acids Research, 45 (4), 2150-2165.
dc.identifier.issn0305-1048es
dc.identifier.urihttp://hdl.handle.net/11441/64082
dc.description.abstractHigher-order plants and mammals use similar mechanisms to repair and tolerate oxidative DNA damage. Most studies on the DNA repair process have focused on yeast and mammals, in which histone chaperone-mediated nucleosome disassembly/reassembly is essential for DNA to be accessible to repair machinery. However, little is known about the specific role and modulation of histone chaperones in the context of DNA damage in plants. Here, the histone chaperone NRP1, which is closely related to human SET/TAF-Iβ, was found to exhibit nucleosome assembly activity in vitro and to accumulate in the chromatin of Arabidopsis thaliana after DNA breaks. In addition, this work establishes that NRP1 binds to cytochrome c, thereby preventing the former from binding to histones. Since NRP1 interacts with cytochrome c at its earmuff domain, that is, its histone-binding domain, cytochrome c thus competes with core histones and hampers the activity of NRP1 as a histone chaperone. Altogether, the results obtained indicate that the underlying molecular mechanisms in nucleosome disassembly/reassembly are highly conserved throughout evolution, as inferred from the similar inhibition of plant NRP1 and human SET/TAF-Iβ by cytochrome c during DNA damage response.es
dc.description.sponsorshipJunta de Andalucía BIO198es
dc.description.sponsorshipMinisterio de Economía y Competitividad BFU2015-71017 / BMC y BFU2013-47064es
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherOxford University Presses
dc.relation.ispartofNucleic Acids Research, 45 (4), 2150-2165.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleHistone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome ces
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO/BFU2015-71017/BMCes
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO/BFU2013-47064es
dc.relation.projectIDBIO198es
dc.relation.publisherversionhttp://dx.doi.org/0.1093/nar/gkw1215es
dc.identifier.doi0.1093/nar/gkw1215es
idus.format.extent16 p.es
dc.journaltitleNucleic Acids Researches
dc.publication.volumen45es
dc.publication.issue4es
dc.publication.initialPage2150es
dc.publication.endPage2165es
dc.contributor.funderJunta de Andalucía
dc.contributor.funderMinisterio de Economía y Competitividad (MINECO). España

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