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http://purl.uniprot.org/citations/10373431http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10373431http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10373431http://www.w3.org/2000/01/rdf-schema#comment"Recently we identified a novel human (h) multiprotein complex, called TATA-binding protein (TBP)-free TAFII-containing complex (TFTC), which is able to nucleate RNA polymerase II transcription and can mediate transcriptional activation. Here we demonstrate that TFTC, similar to other TBP-free TAFII complexes (yeast SAGA, hSTAGA, and hPCAF) contains the acetyltransferase hGCN5 and is able to acetylate histones in both a free and a nucleosomal context. The recently described TRRAP cofactor for oncogenic transcription factor pathways was also characterized as a TFTC subunit. Furthermore, we identified four other previously uncharacterized subunits of TFTC: hADA3, hTAFII150, hSPT3, and hPAF65beta. Thus, the polypeptide composition of TFTC suggests that TFTC is recruited to chromatin templates by activators to acetylate histones and thus may potentiate initiation and activation of transcription."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.26.18285"xsd:string
http://purl.uniprot.org/citations/10373431http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.26.18285"xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/author"Yamamoto K."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/author"Yamamoto K."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/author"Brand M."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/author"Brand M."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/author"Tora L."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/author"Tora L."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/author"Staub A."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/author"Staub A."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/pages"18285-18289"xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/pages"18285-18289"xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/title"Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/title"Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction."xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10373431http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10373431http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10373431
http://purl.uniprot.org/citations/10373431http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10373431