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http://purl.uniprot.org/citations/15664194http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15664194http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15664194http://www.w3.org/2000/01/rdf-schema#comment"The mechanism employed by DNA tumor viruses to inhibit p53-dependent transcription from chromatin is poorly understood. Here, we use in vitro-reconstituted chromatin and UV-irradiated cells to define the mechanism of human papillomavirus E6 oncoprotein in repressing p53-dependent transcription. We demonstrate that E6 does not prevent p53 or p300 recruitment to the chromatin but inhibits p300-mediated acetylation on p53 and nucleosomal core histones. This suppression of protein acetylation requires the E6-interacting regions of p300. Moreover, E6 mutants unable to interact with p53 or p300, but not deficient in inducing p53 degradation, fail to inhibit p53-mediated activation, indicating that a p53-E6-p300-containing protein complex is critical for repressing p53-targeted gene activation. That E6 acts as a molecular switch converting p53-p300 from an activating complex to a repressing entity on the chromatin, which occurs independently of E6AP-mediated protein degradation pathway, may represent a general mechanism for gene regulation."xsd:string
http://purl.uniprot.org/citations/15664194http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2004.12.016"xsd:string
http://purl.uniprot.org/citations/15664194http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2004.12.016"xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/author"Thomas M.C."xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/author"Thomas M.C."xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/author"Chiang C.M."xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/author"Chiang C.M."xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/pages"251-264"xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/pages"251-264"xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/title"E6 oncoprotein represses p53-dependent gene activation via inhibition of protein acetylation independently of inducing p53 degradation."xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/title"E6 oncoprotein represses p53-dependent gene activation via inhibition of protein acetylation independently of inducing p53 degradation."xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/15664194http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/15664194http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15664194
http://purl.uniprot.org/citations/15664194http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15664194
http://purl.uniprot.org/citations/15664194http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15664194
http://purl.uniprot.org/citations/15664194http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15664194
http://purl.uniprot.org/uniprot/P04019http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15664194
http://purl.uniprot.org/uniprot/P04019#attribution-8FFAD3EFEE1F0E92988A62EC595A2898http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15664194