{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Balbo Pogliano C"],"funding":["Swiss National Science Foundation"],"pagination":["1333"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5673894"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(1)"],"pubmed_abstract":["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 i"],"journal":["Nature communications"],"pubmed_title":["ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair."],"pmcid":["PMC5673894"],"funding_grant_id":["170111"],"pubmed_authors":["Garajova Z","Balbo Pogliano C","Naegeli H","Gatti M","Penengo L","Ruthemann P"],"additional_accession":[]},"is_claimable":false,"name":"ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair.","description":"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 i","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Nov","modification":"2026-05-06T03:24:41.086Z","creation":"2019-03-27T03:01:00Z"},"accession":"S-EPMC5673894","cross_references":{"pubmed":["29109511"],"doi":["10.1038/s41467-017-01080-8"]}}