Dissecting the precise role of H3K9 methylation in crosstalk with DNA maintenance methylation in mammals

Nat Commun. 2016 Aug 24:7:12464. doi: 10.1038/ncomms12464.

Abstract

In mammals it is unclear if UHRF1-mediated DNA maintenance methylation by DNMT1 is strictly dependent on histone H3K9 methylation. Here we have generated an Uhrf1 knockin (KI) mouse model that specifically abolishes the H3K9me2/3-binding activity of Uhrf1. The homozygous Uhrf1 KI mice are viable and fertile, and exhibit ∼10% reduction of DNA methylation in various tissues. The reduced DNA methylation occurs globally in the genome and does not restrict only to the H3K9me2/3 enriched repetitive sequences. In vitro UHRF1 binds with higher affinity to reconstituted nucleosome with hemi-methylated CpGs than that with H3K9me2/3, although it binds cooperatively to nucleosome with both modifications. We also show that the nucleosome positioning affects the binding of methylated DNA by UHRF1. Thus, while our study supports a role for H3K9 methylation in promoting DNA methylation, it demonstrates for the first time that DNA maintenance methylation in mammals is largely independent of H3K9 methylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Newborn
  • CCAAT-Enhancer-Binding Proteins
  • CpG Islands / genetics*
  • DNA / genetics
  • DNA / metabolism
  • DNA Methylation*
  • Histones / metabolism*
  • Lysine / metabolism*
  • Mammals / genetics
  • Mammals / metabolism
  • Methylation
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Nucleosomes / genetics
  • Nucleosomes / metabolism
  • Protein Binding
  • Ubiquitin-Protein Ligases

Substances

  • CCAAT-Enhancer-Binding Proteins
  • Histones
  • Nuclear Proteins
  • Nucleosomes
  • DNA
  • Ubiquitin-Protein Ligases
  • Uhrf1 protein, mouse
  • Lysine