BAH domains and a histone-like motif in DNA methyltransferase 1 (DNMT1) regulate de novo and maintenance methylation in vivo
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Title
BAH domains and a histone-like motif in DNA methyltransferase 1 (DNMT1) regulate de novo and maintenance methylation in vivo
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 293, Issue 50, Pages 19466-19475
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2018-10-20
DOI
10.1074/jbc.ra118.004612
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Note: Only part of the references are listed.- Structural and mechanistic insights into UHRF1-mediated DNMT1 activation in the maintenance DNA methylation
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- UHRF1 targets DNMT1 for DNA methylation through cooperative binding of hemi-methylated DNA and methylated H3K9
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- Structure of DNMT1-DNA Complex Reveals a Role for Autoinhibition in Maintenance DNA Methylation
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- Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism
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