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dc.contributor.authorFranco Arana, Aitor
dc.contributor.authorArranz, Rocio
dc.contributor.authorFernández Rivero, Noelia
dc.contributor.authorVelázquez Campoy, Adrián
dc.contributor.authorMartín Benito, Jaime
dc.contributor.authorSegura, Joan
dc.contributor.authorPrado Ruiz, Adelina
dc.contributor.authorValpuesta, José M.
dc.contributor.authorMuga Villate, Arturo
dc.date.accessioned2020-03-11T09:46:41Z
dc.date.available2020-03-11T09:46:41Z
dc.date.issued2019-07-01
dc.identifier.citationScientific Reports 9 : (2019) // Article ID 9487es_ES
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/10810/42092
dc.description.abstractNucleoplasmin (NP) is a pentameric histone chaperone that regulates the condensation state of chromatin in different cellular processes. We focus here on the interaction of NP with the histone octamer, showing that NP could bind sequentially the histone components to assemble an octamer-like particle, and crosslinked octamers with high affinity. The three-dimensional reconstruction of the NP/octamer complex generated by single-particle cryoelectron microscopy, revealed that several intrinsically disordered tail domains of two NP pentamers, facing each other through their distal face, encage the histone octamer in a nucleosome-like conformation and prevent its dissociation. Formation of this complex depended on post-translational modification and exposure of the acidic tract at the tail domain of NP. Finally, NP was capable of transferring the histone octamers to DNA in vitro, assembling nucleosomes. This activity may have biological relevance for processes in which the histone octamer must be rapidly removed from or deposited onto the DNA.es_ES
dc.description.sponsorshipWe thank the LMB staff, in particular Drs Shaoxia Chen and Christos Savva, for the use of the Titan Krios. N.F.R. and A.F. thank the Basque Government for their predoctoral fellowships. Also, the excellent technical assistance of N. Orozco is gratefully acknowledged. The professional editing service NB Revisions was used for technical preparation of the text prior to submission. This work was supported by Agencia Espanola de Investigacion/Fondos de Desarrollo Regional (AEI/FEDER, UE), [BFU2016-75984 to J.M.V., BFU2016-75983 to A.M.] and the Basque Government [IT709-13 to A.M.].es_ES
dc.language.isoenges_ES
dc.publisherNature Publishing Groupes_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es/*
dc.subjectchromatin decondensationes_ES
dc.subjectcrystal-structurees_ES
dc.subjectsperm chromatines_ES
dc.subjectacidic proteines_ES
dc.subjectnucleosomees_ES
dc.subjectcorees_ES
dc.subjecttranscriptiones_ES
dc.subjectmechanismes_ES
dc.subjectcomplexeses_ES
dc.subjecttetrameres_ES
dc.titleStructural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA depositiones_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.holderThis article is licensed under a Creative Commons Attribution 4.0 International License. (CC BY 4.0)es_ES
dc.rights.holderAtribución 3.0 España*
dc.relation.publisherversionhttps://www.nature.com/articles/s41598-019-45726-7es_ES
dc.identifier.doi10.1038/s41598-019-45726-7
dc.departamentoesBioquímica y biología moleculares_ES
dc.departamentoeuBiokimika eta biologia molekularraes_ES


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This article is licensed under a Creative Commons Attribution 4.0 International License. (CC BY 4.0)
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