{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xu TH"],"funding":["NCI NIH HHS"],"pagination":["151-155"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7540737"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["586(7827)"],"pubmed_abstract":["CpG methylation by de novo DNA methyltransferases (DNMTs) 3A and 3B is essential for mammalian development and differentiation and is frequently dysregulated in cancer<sup>1</sup>. These two DNMTs preferentially bind to nucleosomes, yet cannot methylate the DNA wrapped around the nucleosome core<sup>2</sup>, and they favour the methylation of linker DNA at positioned nucleosomes<sup>3,4</sup>. Here we present the cryo-electron microscopy structure of a ternary complex of catalytically competent DNMT3A2, the catalytically inactive accessory subunit DNMT3B3 and a nucleosome core particle flanked by linker DNA. The catalytic-like domain of the accessory DNMT3B3 binds to the acidic patch of the nucleosome core, which orients the binding of DNMT3A2 to the linker DNA. The steric constraints of t"],"journal":["Nature"],"pubmed_title":["Structure of nucleosome-bound DNA methyltransferases DNMT3A and DNMT3B."],"pmcid":["PMC7540737"],"funding_grant_id":["R50 CA243878","R35 CA209859"],"pubmed_authors":["Zhou XE","Liang G","Liu M","Melcher K","Zhao G","Jones PA","Xu TH","Xu HE"],"additional_accession":[]},"is_claimable":false,"name":"Structure of nucleosome-bound DNA methyltransferases DNMT3A and DNMT3B.","description":"CpG methylation by de novo DNA methyltransferases (DNMTs) 3A and 3B is essential for mammalian development and differentiation and is frequently dysregulated in cancer<sup>1</sup>. These two DNMTs preferentially bind to nucleosomes, yet cannot methylate the DNA wrapped around the nucleosome core<sup>2</sup>, and they favour the methylation of linker DNA at positioned nucleosomes<sup>3,4</sup>. Here we present the cryo-electron microscopy structure of a ternary complex of catalytically competent DNMT3A2, the catalytically inactive accessory subunit DNMT3B3 and a nucleosome core particle flanked by linker DNA. The catalytic-like domain of the accessory DNMT3B3 binds to the acidic patch of the nucleosome core, which orients the binding of DNMT3A2 to the linker DNA. The steric constraints of t","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2026-05-09T00:39:13.882Z","creation":"2025-02-19T02:13:14.99Z"},"accession":"S-EPMC7540737","cross_references":{"pubmed":["32968275"],"doi":["10.1038/s41586-020-2747-1"]}}