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Article

Structural basis for activation of DNMT1

2022-06-17

Abstract excerpt

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 conser...

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Identifiers and source

Literature Corpus work
91a76c11-78ae-55f9-9dcc-3f168532d59c
DOI
10.1101/2022.06.16.496385
Open publication

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Structural basis for activation of DNMT1DOI 10.1101/2022.06.16.496385
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