{"doi":"10.1126/science.abc6663","title":"Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation","abstract":"<jats:title>Cross-talk between histone modifications</jats:title>\n          <jats:p>\n            Histone modifications play pivotal roles within the intricate protein networks that underlie transcription and gene silencing in eukaryotic genomes. The enzymes that deposit them undergo spatiotemporal fine-tuning of their catalytic activity; one example is trans-histone cross-talk, in which one histone modification activates an enzyme responsible for another histone modification. Valencia-Sánchez\n            <jats:italic>et al.</jats:italic>\n            show that histone H4 lysine 16 acetylation (H4K16ac), a hallmark of decondensed, transcriptionally permissive chromatin, directly stimulates the Dot1 histone H3 lysine 79 methyltransferase. Structural, biochemical, and cellular data explain Dot1's regulation by H4K16ac and show how it coordinates with a second positive regulator of Dot1, histone H2B ubiquitination.\n          </jats:p>\n          <jats:p>\n            <jats:italic>Science</jats:italic>\n            , this issue p.\n            <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" related-article-type=\"in-this-issue\" xlink:href=\"10.1126/science.abc6663\">eabc6663</jats:related-article>\n          </jats:p>","journal":"Science","year":2021,"id":20614,"datarank":2.9957286940176853,"base_score":4.7535901911063645,"endowment":4.7535901911063645,"self_citation_contribution":0.7130385286659547,"citation_network_contribution":2.2826901653517306,"self_endowment_contribution":0.7130385286659547,"citer_contribution":2.2826901653517306,"corpus_percentile":null,"corpus_rank":null,"citation_count":115,"citer_count":105,"citers_with_citation_signal":85,"citers_with_endowment":85,"datacite_reuse_total":4,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":135645,"name":"Pablo De Ioannes","orcid":"0000-0003-1944-3912","position":1,"is_corresponding":false},{"id":135646,"name":"Miao Wang","orcid":"0000-0002-9193-3142","position":2,"is_corresponding":false},{"id":135647,"name":"David M. Truong","orcid":"0000-0002-5121-5111","position":3,"is_corresponding":false},{"id":135648,"name":"Rachel Lee","orcid":"0000-0003-2501-5973","position":4,"is_corresponding":false},{"id":98191,"name":"Jean‐Paul Armache","orcid":"0000-0001-9195-2282","position":5,"is_corresponding":false},{"id":49826,"name":"Jef D. Boeke","orcid":"0000-0001-5322-4946","position":6,"is_corresponding":false},{"id":135649,"name":"Karim-Jean Armache","orcid":"0000-0002-0890-9513","position":7,"is_corresponding":false},{"id":135644,"name":"Marco Igor Valencia-Sánchez","orcid":"0000-0002-7199-4546","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":4.7535901911063645,"endowment":4.7535901911063645,"datacite_reuse_total":4,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"33479126","pmcid":"PMC8279004","openalex_id":"https://openalex.org/W3123057917","authors":[],"funders":[{"funder_name":"National Science Foundation","grant_id":"MCB-1921641","title":null},{"funder_name":"National Institutes of Health","grant_id":"5R01GM115882","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM115882","title":null},{"funder_name":"National Science Foundation","grant_id":"1921641","title":"URoL:  Epigenetics 2:  Reverse Engineering Human Epigenetic Machinery in Yeast"},{"funder_name":"National Institutes of Health","grant_id":"3R01GM115882-02S1","title":"Structural and functional analysis of gene silencing"},{"funder_name":"David and Lucile Packard Foundation","grant_id":"","title":null}],"total_grants":6,"fwci":7.5712,"citation_percentile":0.98347998,"influential_citations":4,"citation_trend":[{"year":2021,"count":17},{"year":2022,"count":24},{"year":2023,"count":25},{"year":2024,"count":27},{"year":2025,"count":9},{"year":2026,"count":13}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/8279004","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8279004","host_type":"GREEN"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/8279004","host_type":"repository"},{"url":"https://syndication.highwire.org/content/doi/10.1126/science.abc6663","host_type":"publisher"},{"url":"https://www.science.org/doi/pdf/10.1126/science.abc6663","host_type":"publisher"},{"url":"https://doi.org/10.1126/science.abc6663","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/33479126","host_type":"repository"},{"url":"https://dx.doi.org/10.1126/science.abc6663","host_type":""}],"fields_of_study":["Genomics and Chromatin Dynamics","RNA modifications and cancer","Ubiquitin and proteasome pathways","Medicine","Biology","Chemistry","Acetylation","Chromatin Assembly and Disassembly","Histone-Lysine N-Methyltransferase","Histones","Nuclear Proteins","Nucleosomes","Protein Conformation","Protein Processing, Post-Translational","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins"],"mesh_terms":["Acetylation","Histones","Nuclear Proteins","Nucleosomes","Protein Conformation","Histone-Lysine N-Methyltransferase","Protein Processing, Post-Translational","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins","Chromatin Assembly and Disassembly"],"keywords":["Histone methyltransferase","Histone code","Histone H2A","Histone H1","Histone H3","Histone methylation","Biology","Histone H4","Histone octamer","Histone","Cell biology","Biochemistry","Gene expression","Nucleosome","DNA","Gene","DNA methylation","Histones","Saccharomyces cerevisiae Proteins","Protein Conformation","Nuclear Proteins","Acetylation","Histone-Lysine N-Methyltransferase","Saccharomyces cerevisiae","Chromatin Assembly and Disassembly","Protein Processing, Post-Translational","Nucleosomes"],"sdg_mappings":[{"sdg_number":2,"sdg_label":"2. 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Good health"}],"linked_datasets":[{"doi":"10.6084/m9.figshare.26628328","title":"Additional file 1 of Unveiling the role of GAS41 in cancer progression","publisher":"figshare","resource_type":"Image"},{"doi":"10.6084/m9.figshare.26628331.v1","title":"Additional file 2 of Unveiling the role of GAS41 in cancer progression","publisher":"figshare","resource_type":"Image"},{"doi":"10.6084/m9.figshare.26628328.v1","title":"Additional file 1 of Unveiling the role of GAS41 in cancer progression","publisher":"figshare","resource_type":"Image"},{"doi":"10.6084/m9.figshare.26628331","title":"Additional file 2 of Unveiling the role of GAS41 in cancer progression","publisher":"figshare","resource_type":"Image"}],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"emdb"},{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-06T04:20:36.052609Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}