Regulation of maintenance DNA methylation via histone ubiquitylation

J Biochem. 2016 Jan;159(1):9-15. doi: 10.1093/jb/mvv113. Epub 2015 Nov 20.

Abstract

DNA methylation is one of the most stable but dynamically regulated epigenetic marks that act as determinants of cell fates during embryonic development through regulation of various forms of gene expression. DNA methylation patterns must be faithfully propagated throughout successive cell divisions in order to maintain cell-specific function. We have recently demonstrated that Uhrf1-dependent ubiquitylation of histone H3 at lysine 23 is critical for Dnmt1 recruitment to DNA replication sites, which catalyzes the conversion of hemi-methylated DNA to fully methylated DNA. In this review, we provide an overview of recent progress in understanding the mechanism underlying maintenance DNA methylation.

Keywords: DNA methylation; DNA methyltransferase 1, histone; Ubiquitin; cell cycle.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • CCAAT-Enhancer-Binding Proteins / metabolism*
  • Cell Cycle
  • Cell Differentiation
  • Cell-Free System
  • CpG Islands / genetics
  • DNA (Cytosine-5-)-Methyltransferase 1
  • DNA (Cytosine-5-)-Methyltransferases / metabolism*
  • DNA Methylation*
  • DNA Replication
  • Epigenesis, Genetic*
  • Histones / genetics
  • Histones / metabolism*
  • Humans
  • Lysine / metabolism
  • RING Finger Domains
  • Ubiquitin Thiolesterase / metabolism
  • Ubiquitin-Protein Ligases
  • Ubiquitin-Specific Peptidase 7
  • Ubiquitination* / genetics
  • Xenopus

Substances

  • CCAAT-Enhancer-Binding Proteins
  • Histones
  • DNA (Cytosine-5-)-Methyltransferase 1
  • DNA (Cytosine-5-)-Methyltransferases
  • DNMT1 protein, human
  • UHRF1 protein, human
  • Ubiquitin-Protein Ligases
  • USP7 protein, human
  • Ubiquitin Thiolesterase
  • Ubiquitin-Specific Peptidase 7
  • Lysine