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dc.contributor.authorGarcía, Alicia-
dc.contributor.authorRosonina, Emanuel-
dc.contributor.authorManley, James L.-
dc.contributor.authorCalvo, Olga-
dc.date.accessioned2012-01-26T14:15:17Z-
dc.date.available2012-01-26T14:15:17Z-
dc.date.issued2010-11-
dc.identifier.citationMolecular and Cellular Biology 30(21): 5180-5193 (2010)es_ES
dc.identifier.issn0270-7306-
dc.identifier.urihttp://hdl.handle.net/10261/44813-
dc.description.abstractThe transcriptional coactivator Sub1 has been implicated in several aspects of mRNA metabolism in yeast, such as activation of transcription, termination, and 3′-end formation. Here, we present evidence that Sub1 plays a significant role in controlling phosphorylation of the RNA polymerase II large subunit C-terminal domain (CTD). We show that SUB1 genetically interacts with the genes encoding all four known CTD kinases, SRB10, KIN28, BUR1, and CTK1, suggesting that Sub1 acts to influence CTD phosphorylation at more than one step of the transcription cycle. To address this directly, we first used in vitro kinase assays, and we show that, on the one hand, SUB1 deletion increased CTD phosphorylation by Kin28, Bur1, and Ctk1 but, on the other, it decreased CTD phosphorylation by Srb10. Second, chromatin immunoprecipitation assays revealed that SUB1 deletion decreased Srb10 chromatin association on the inducible GAL1 gene but increased Kin28 and Ctk1 chromatin association on actively transcribed genes. Taken together, our data point to multiple roles for Sub1 in the regulation of CTD phosphorylation throughout the transcription cycle.es_ES
dc.description.sponsorshipThis work was supported by grants number BFU 2006-09041 and BFU 2009-07179 from the Spanish Ministerio de Ciencia e Innovación and SA012A08 from the Junta de Castilla y León to O.C. and a grant from the NIH to J.L.M. A.G. was supported by a fellowship from the Junta de Castilla y León.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Microbiologyes_ES
dc.rightsclosedAccesses_ES
dc.titleSub1 globally regulates RNA polymerase II C-terminal domain phosphorylationes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1128/​MCB.00819-10-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1128/MCB.00819-10es_ES
dc.identifier.e-issn1098-5549-
dc.contributor.funderJunta de Castilla y León-
dc.contributor.funderMinisterio de Ciencia e Innovación (España)-
dc.contributor.funderNational Institutes of Health (US)-
dc.identifier.funderhttp://dx.doi.org/10.13039/100000002es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100004837es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100014180es_ES
dc.identifier.pmid20823273-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairetypeartículo-
item.cerifentitytypePublications-
item.languageiso639-1en-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
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