{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yan J"],"funding":["National Natural Science Foundation of China","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["8"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9852454"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(1)"],"pubmed_abstract":["N<sup>6</sup>-methyldeoxyadenine (6mA) has recently been reported as a prevalent DNA modification in eukaryotes. The Tetrahymena thermophila MTA1 complex consisting of four subunits, namely MTA1, MTA9, p1, and p2, is the first identified eukaryotic 6mA methyltransferase (MTase) complex. Unlike the prokaryotic 6mA MTases which have been biochemically and structurally characterized, the operation mode of the MTA1 complex remains largely elusive. Here, we report the cryogenic electron microscopy structures of the quaternary MTA1 complex in S-adenosyl methionine (SAM)-bound (2.6 Å) and S-adenosyl homocysteine (SAH)-bound (2.8 Å) states. Using an AI-empowered integrative approach based on AlphaFold prediction and chemical cross-linking mass spectrometry, we further modeled a near-complete struc"],"journal":["Cell discovery"],"pubmed_title":["Structural insights into DNA N<sup>6</sup>-adenine methylation by the MTA1 complex."],"pmcid":["PMC9852454"],"funding_grant_id":["32130011"],"pubmed_authors":["Liu Z","Yan J","Guan Z","Jin X","Zhang D","Wang Q","Wu S","Yin P","Yan X","Wang Z","Liu F"],"additional_accession":[]},"is_claimable":false,"name":"Structural insights into DNA N<sup>6</sup>-adenine methylation by the MTA1 complex.","description":"N<sup>6</sup>-methyldeoxyadenine (6mA) has recently been reported as a prevalent DNA modification in eukaryotes. The Tetrahymena thermophila MTA1 complex consisting of four subunits, namely MTA1, MTA9, p1, and p2, is the first identified eukaryotic 6mA methyltransferase (MTase) complex. Unlike the prokaryotic 6mA MTases which have been biochemically and structurally characterized, the operation mode of the MTA1 complex remains largely elusive. Here, we report the cryogenic electron microscopy structures of the quaternary MTA1 complex in S-adenosyl methionine (SAM)-bound (2.6 Å) and S-adenosyl homocysteine (SAH)-bound (2.8 Å) states. Using an AI-empowered integrative approach based on AlphaFold prediction and chemical cross-linking mass spectrometry, we further modeled a near-complete struc","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-05-28T13:54:14.71Z","creation":"2025-02-19T01:08:26.357Z"},"accession":"S-EPMC9852454","cross_references":{"pubmed":["36658132"],"doi":["10.1038/s41421-022-00516-w"]}}