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  2. FCEN
  3. FCEN - Facultad de Ciencias Exactas y Naturales. UBA
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dc.provenanceFacultad de Ciencias Exactas y Naturales de la UBA-
dc.contributor<div class="autor_fcen" id="7966">Schor, I.E.</div>-
dc.contributorLlères, D.-
dc.contributor<div class="autor_fcen" id="7285">Risso, G.J.</div>-
dc.contributorPawellek, A.-
dc.contributorUle, J.-
dc.contributorLamond, A.I.-
dc.contributor<div class="autor_fcen" id="4634">Kornblihtt, A.R.</div>-
dc.creator<div class="autor_fcen" id="7966">Schor, I.E.</div>-
dc.creatorLlères, D.-
dc.creator<div class="autor_fcen" id="7285">Risso, G.J.</div>-
dc.creatorPawellek, A.-
dc.creatorUle, J.-
dc.creatorLamond, A.I.-
dc.creator<div class="autor_fcen" id="4634">Kornblihtt, A.R.</div>-
dc.date.accessioned2018-05-04T22:06:36Z-
dc.date.accessioned2018-05-28T15:49:11Z-
dc.date.available2018-05-04T22:06:36Z-
dc.date.available2018-05-28T15:49:11Z-
dc.date.issued2012-
dc.identifier.urihttp://10.0.0.11:8080/jspui/handle/bnmm/68616-
dc.descriptionChromatin structure is an important factor in the functional coupling between transcription and mRNA processing, not only by regulating alternative splicing events, but also by contributing to exon recognition during constitutive splicing. We observed that depolarization of neuroblastoma cell membrane potential, which triggers general histone acetylation and regulates alternative splicing, causes a concentration of SR proteins in nuclear speckles. This prompted us to analyze the effect of chromatin structure on splicing factor distribution and dynamics. Here, we show that induction of histone hyper-acetylation results in the accumulation in speckles of multiple splicing factors in different cell types. In addition, a similar effect is observed after depletion of the heterochromatic protein HP1α, associated with repressive chromatin. We used advanced imaging approaches to analyze in detail both the structural organization of the speckle compartment and nuclear distribution of splicing factors, as well as studying direct interactions between splicing factors and their association with chromatin in vivo. The results support a model where perturbation of normal chromatin structure decreases the recruitment efficiency of splicing factors to nascent RNAs, thus causing their accumulation in speckles, which buffer the amount of free molecules in the nucleoplasm. To test this, we analyzed the recruitment of the general splicing factor U2AF65 to nascent RNAs by iCLIP technique, as a way to monitor early spliceosome assembly. We demonstrate that indeed histone hyper-acetylation decreases recruitment of U2AF65 to bulk 3′ splice sites, coincident with the change in its localization. In addition, prior to the maximum accumulation in speckles, ~20% of genes already show a tendency to decreased binding, while U2AF65 seems to increase its binding to the speckle-located ncRNA MALAT1. All together, the combined imaging and biochemical approaches support a model where chromatin structure is essential for efficient co-transcriptional recruitment of general and regulatory splicing factors to pre-mRNA. © 2012 Schor et al.-
dc.descriptionFil:Schor, I.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.descriptionFil:Risso, G.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.descriptionFil:Kornblihtt, A.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.formatapplication/pdf-
dc.languageeng-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttp://creativecommons.org/licenses/by/2.5/ar-
dc.sourcePLoS ONE 2012;7(11)-
dc.source.urihttp://digital.bl.fcen.uba.ar/Download/paper/paper_19326203_v7_n11_p_Schor.pdf-
dc.subjectenhanced green fluorescent protein-
dc.subjectheterochromatin protein 1-
dc.subjectheterochromatin protein 1alpha-
dc.subjecthistone H3-
dc.subjecthistone H4-
dc.subjectmessenger RNA-
dc.subjectnuclear protein-
dc.subjectprotein SRSF1-
dc.subjectprotein SRSF2-
dc.subjecttrichostatin A-
dc.subjectunclassified drug-
dc.subjectuntranslated RNA-
dc.subjectarticle-
dc.subjectbioaccumulation-
dc.subjectcell nucleus-
dc.subjectcellular distribution-
dc.subjectchromatin structure-
dc.subjectcontrolled study-
dc.subjectgene control-
dc.subjectgene function-
dc.subjecthistone acetylation-
dc.subjecthuman-
dc.subjecthuman cell-
dc.subjectMALAT1 gene-
dc.subjectmolecular imaging-
dc.subjectmolecular model-
dc.subjectNCAM gene-
dc.subjectNeat1 gene-
dc.subjectprotein determination-
dc.subjectprotein function-
dc.subjectprotein RNA binding-
dc.subjectregulatory mechanism-
dc.subjectRNA analysis-
dc.subjectRNA gene-
dc.subjectRNA splicing-
dc.subjectspliceosome-
dc.subjectstructure analysis-
dc.subjectAcetylation-
dc.subjectAlternative Splicing-
dc.subjectAnimals-
dc.subjectCell Line-
dc.subjectCell Nucleus-
dc.subjectChromatin-
dc.subjectHistones-
dc.subjectHumans-
dc.subjectHydroxamic Acids-
dc.subjectMembrane Potentials-
dc.subjectModels, Biological-
dc.subjectProtein Binding-
dc.subjectProtein Transport-
dc.subjectRibonucleoproteins-
dc.subjectRNA Precursors-
dc.subjectRNA Splice Sites-
dc.subjectRNA Splicing-
dc.subjectRNA, Long Untranslated-
dc.titlePerturbation of Chromatin Structure Globally Affects Localization and Recruitment of Splicing Factors-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:ar-repo/semantics/artículo-
dc.typeinfo:eu-repo/semantics/publishedVersion-
Aparece en las colecciones: FCEN - Facultad de Ciencias Exactas y Naturales. UBA

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