{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen X"],"funding":["U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences","U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS)","NIEHS NIH HHS","U.S. Department of Health & Human Services | NIH | National Cancer Institute","U.S. Department of Health & Human Services | NIH | National Institute of Environmental Health Sciences","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["6217"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11266573"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Isoform 1 of DNA methyltransferase DNMT3A (DNMT3A1) specifically recognizes nucleosome monoubiquitylated at histone H2A lysine-119 (H2AK119ub1) for establishment of DNA methylation. Mis-regulation of this process may cause aberrant DNA methylation and pathogenesis. However, the molecular basis underlying DNMT3A1-nucleosome interaction remains elusive. Here we report the cryo-EM structure of DNMT3A1's ubiquitin-dependent recruitment (UDR) fragment complexed with H2AK119ub1-modified nucleosome. DNMT3A1 UDR occupies an extensive nucleosome surface, involving the H2A-H2B acidic patch, a surface groove formed by H2A and H3, nucleosomal DNA, and H2AK119ub1. The DNMT3A1 UDR's interaction with H2AK119ub1 affects the functionality of DNMT3A1 in cells in a context-dependent manner. Our structural an"],"journal":["Nature communications"],"pubmed_title":["Structural basis for the H2AK119ub1-specific DNMT3A-nucleosome interaction."],"pmcid":["PMC11266573"],"funding_grant_id":["R01 GM129325","R01 CA215284","R35 ES031707","U24 GM129539","R35 GM119721","R01 CA211336","R35GM119721"],"pubmed_authors":["Fang J","Guo Y","Lu J","Chen X","Zhao T","Wang Y","Wang GG","Song J"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis for the H2AK119ub1-specific DNMT3A-nucleosome interaction.","description":"Isoform 1 of DNA methyltransferase DNMT3A (DNMT3A1) specifically recognizes nucleosome monoubiquitylated at histone H2A lysine-119 (H2AK119ub1) for establishment of DNA methylation. Mis-regulation of this process may cause aberrant DNA methylation and pathogenesis. However, the molecular basis underlying DNMT3A1-nucleosome interaction remains elusive. Here we report the cryo-EM structure of DNMT3A1's ubiquitin-dependent recruitment (UDR) fragment complexed with H2AK119ub1-modified nucleosome. DNMT3A1 UDR occupies an extensive nucleosome surface, involving the H2A-H2B acidic patch, a surface groove formed by H2A and H3, nucleosomal DNA, and H2AK119ub1. The DNMT3A1 UDR's interaction with H2AK119ub1 affects the functionality of DNMT3A1 in cells in a context-dependent manner. Our structural an","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-02T05:04:31.578Z","creation":"2025-04-19T13:10:59.176Z"},"accession":"S-EPMC11266573","cross_references":{"pubmed":["39043678"],"doi":["10.1038/s41467-024-50526-3"]}}