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http://purl.uniprot.org/citations/21358630http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21358630http://www.w3.org/2000/01/rdf-schema#comment"Pre-messenger RNAs (pre-mRNAs) maturation is initiated cotranscriptionally. It is therefore conceivable that chromatin-borne information participates in alternative splicing. Here we find that elevated levels of trimethylation of histone H3 on Lys9 (H3K9me3) are a characteristic of the alternative exons of several genes including CD44. On this gene the chromodomain protein HP1γ, frequently defined as a transcriptional repressor, facilitates inclusion of the alternative exons via a mechanism involving decreased RNA polymerase II elongation rate. In addition, accumulation of HP1γ on the variant region of the CD44 gene stabilizes association of the pre-mRNA with the chromatin. Altogether, our data provide evidence for localized histone modifications impacting alternative splicing. They further implicate HP1γ as a possible bridging molecule between the chromatin and the maturating mRNA, with a general impact on splicing decisions."xsd:string
http://purl.uniprot.org/citations/21358630http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.1995"xsd:string
http://purl.uniprot.org/citations/21358630http://purl.uniprot.org/core/author"Batsche E."xsd:string
http://purl.uniprot.org/citations/21358630http://purl.uniprot.org/core/author"Muchardt C."xsd:string
http://purl.uniprot.org/citations/21358630http://purl.uniprot.org/core/author"Rachez C."xsd:string
http://purl.uniprot.org/citations/21358630http://purl.uniprot.org/core/author"Saint-Andre V."xsd:string
http://purl.uniprot.org/citations/21358630http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21358630http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/21358630http://purl.uniprot.org/core/pages"337-344"xsd:string
http://purl.uniprot.org/citations/21358630http://purl.uniprot.org/core/title"Histone H3 lysine 9 trimethylation and HP1gamma favor inclusion of alternative exons."xsd:string
http://purl.uniprot.org/citations/21358630http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/21358630http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21358630
http://purl.uniprot.org/citations/21358630http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21358630
http://purl.uniprot.org/uniprot/#_B8ZZ43-mappedCitation-21358630http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21358630
http://purl.uniprot.org/uniprot/#_Q13185-mappedCitation-21358630http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21358630
http://purl.uniprot.org/uniprot/Q13185http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21358630
http://purl.uniprot.org/uniprot/B8ZZ43http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21358630