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http://purl.uniprot.org/citations/29109511http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29109511http://www.w3.org/2000/01/rdf-schema#comment"Global-genome nucleotide excision repair (GG-NER) prevents ultraviolet (UV) light-induced skin cancer by removing mutagenic cyclobutane pyrimidine dimers (CPDs). These lesions are formed abundantly on DNA wrapped around histone octamers in nucleosomes, but a specialized damage sensor known as DDB2 ensures that they are accessed by the XPC initiator of GG-NER activity. We report that DDB2 promotes CPD excision by recruiting the histone methyltransferase ASH1L, which methylates lysine 4 of histone H3. In turn, methylated H3 facilitates the docking of the XPC complex to nucleosomal histone octamers. Consequently, DDB2, ASH1L and XPC proteins co-localize transiently on histone H3-methylated nucleosomes of UV-exposed cells. In the absence of ASH1L, the chromatin binding of XPC is impaired and its ability to recruit downstream GG-NER effectors diminished. Also, ASH1L depletion suppresses CPD excision and confers UV hypersensitivity. These findings show that ASH1L configures chromatin for the effective handoff between damage recognition factors during GG-NER activity."xsd:string
http://purl.uniprot.org/citations/29109511http://purl.org/dc/terms/identifier"doi:10.1038/s41467-017-01080-8"xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/author"Gatti M."xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/author"Naegeli H."xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/author"Penengo L."xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/author"Garajova Z."xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/author"Ruthemann P."xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/author"Balbo Pogliano C."xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/pages"1333"xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/title"ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair."xsd:string
http://purl.uniprot.org/citations/29109511http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/29109511http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/29109511
http://purl.uniprot.org/citations/29109511http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/29109511
http://purl.uniprot.org/uniprot/#_A0A7I2V316-mappedCitation-29109511http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29109511
http://purl.uniprot.org/uniprot/#_A0A7I2V3D6-mappedCitation-29109511http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29109511
http://purl.uniprot.org/uniprot/#_B4E3U8-mappedCitation-29109511http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29109511
http://purl.uniprot.org/uniprot/#_Q9NR48-mappedCitation-29109511http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29109511
http://purl.uniprot.org/uniprot/Q9NR48http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29109511
http://purl.uniprot.org/uniprot/A0A7I2V3D6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29109511
http://purl.uniprot.org/uniprot/A0A7I2V316http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29109511
http://purl.uniprot.org/uniprot/B4E3U8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29109511