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dc.creatorGonzález Arzola, Katiuskaes
dc.creatorDíaz Moreno, Irenees
dc.creatorCano González, Ana Maríaes
dc.creatorDíaz Quintana, Antonio Jesúses
dc.creatorVelázquez Campoy, Adriánes
dc.creatorMoreno Beltrán, José Blases
dc.creatorLópez Rivas, Abelardoes
dc.creatorRosa Acosta, Miguel Ángel de laes
dc.date.accessioned2018-01-12T12:12:30Z
dc.date.available2018-01-12T12:12:30Z
dc.date.issued2015
dc.identifier.citationGonzález Arzola, K., Díaz Moreno, I., Cano González, A.M., Díaz Quintana, A.J., Velázquez Campoy, A., Moreno Beltrán, B.,...,Rosa Acosta, M.Á.d.l. (2015). Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c. Proceedings of the National Academy of Sciences, 112 (32), 9908-9913.
dc.identifier.issn0027-8424es
dc.identifier.urihttp://hdl.handle.net/11441/68902
dc.description.abstractChromatin is pivotal for regulation of the DNA damage process insofar as it influences access to DNA and serves as a DNA repair docking site. Recent works identify histone chaperones as key regulators of damaged chromatin’s transcriptional activity. However, understanding how chaperones are modulated during DNA damage response is still challenging. This study reveals that the histone chaperone SET/TAF-Iβ interacts with cytochrome c following DNA damage. Specifically, cytochrome c is shown to be translocated into cell nuclei upon induction of DNA damage, but not upon stimulation of the death receptor or stress-induced pathways. Cytochrome c was found to competitively hinder binding of SET/TAF-Iβ to core histones, thereby locking its histone-binding domains and inhibiting its nucleosome assembly activity. In addition, we have used NMR spectroscopy, calorimetry, mutagenesis, and molecular docking to provide an insight into the structural features of the formation of the complex between cytochrome c and SET/TAF-Iβ. Overall, these findings establish a framework for understanding the molecular basis of cytochrome c-mediated blocking of SET/TAF-Iβ, which subsequently may facilitate the development of new drugs to silence the oncogenic effect of SET/TAF-Iβ’s histone chaperone activity.es
dc.description.sponsorshipEspaña Mineco FU2012-31670, BFU2010-19451, BFU2013- 47064-P, SAF2012-32824, RD12/0036/002es
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherNational Academy of Scienceses
dc.relation.ispartofProceedings of the National Academy of Sciences, 112 (32), 9908-9913.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectCytochrome ces
dc.subjectHistone chaperonees
dc.subjectITCes
dc.subjectNMRes
dc.subjectSET-TAF-Iβes
dc.titleStructural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome ces
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/submittedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Moleculares
dc.relation.projectIDFU2012-31670es
dc.relation.projectIDBFU2010-19451es
dc.relation.projectIDBFU2013- 47064-Pes
dc.relation.projectIDSAF2012-32824es
dc.relation.projectIDRD12/0036/002es
dc.relation.publisherversionhttp://dx.doi.org/10.1073/pnas.1508040112es
dc.identifier.doi10.1073/pnas.1508040112es
idus.format.extent5 p.es
dc.journaltitleProceedings of the National Academy of Scienceses
dc.publication.volumen112es
dc.publication.issue32es
dc.publication.initialPage9908es
dc.publication.endPage9913es
dc.contributor.funderMinisterio de Economía y Competitividad (MINECO). España

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