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- W4283021311 abstract "Abstract DNMT1 is an essential enzyme that maintains genomic DNA methylation, and its function is regulated by mechanisms that are not yet fully understood. Here, we report the cryo-EM structure of human DNMT1 bound to its two natural activators: hemimethylated DNA and ubiquitinated histone H3. We find that a hitherto unstudied linker, between the RFTS and CXXC domains, plays a key role for activation. It contains a conserved α-helix which engages a crucial Toggle pocket, displacing a previously described inhibitory linker, and allowing the DNA recognition helix to spring into the active conformation. This is accompanied by large-scale reorganization of the inhibitory RFTS and CXXC domains, allowing the enzyme to gain full activity. Our results therefore provide a mechanistic basis for the activation of DNMT1, with consequences for basic research and drug design." @default.
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- W4283021311 date "2022-06-17" @default.
- W4283021311 modified "2023-10-18" @default.
- W4283021311 title "Structural basis for activation of DNMT1" @default.
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- W4283021311 doi "https://doi.org/10.1101/2022.06.16.496385" @default.
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