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Uracil-DNA Glycosylase UNG Promotes Tet-mediated DNA Demethylation

J Biol Chem. 2016 Jan 8;291(2):731-8. doi: 10.1074/jbc.M115.693861. Epub 2015 Nov 30.

Abstract

In mammals, active DNA demethylation involves oxidation of 5-methylcytosine (5mC) into 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) by Tet dioxygenases and excision of these two oxidized bases by thymine DNA glycosylase (TDG). Although TDG is essential for active demethylation in embryonic stem cells and induced pluripotent stem cells, it is hardly expressed in mouse zygotes and dispensable in pronuclear DNA demethylation. To search for other factors that might contribute to demethylation in mammalian cells, we performed a functional genomics screen based on a methylated luciferase reporter assay. UNG2, one of the glycosylases known to excise uracil residues from DNA, was found to reduce DNA methylation, thus activating transcription of a methylation-silenced reporter gene when co-transfected with Tet2 into HEK293T cells. Interestingly, UNG2 could decrease 5caC from the genomic DNA and a reporter plasmid in transfected cells, like TDG. Furthermore, deficiency in Ung partially impaired DNA demethylation in mouse zygotes. Our results suggest that UNG might be involved in Tet-mediated DNA demethylation.

Keywords: DNA demethylation; DNA methylation; Tet; UNG2; base excision repair (BER); gene knockout; transcription regulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cytosine / analogs & derivatives
  • DNA / metabolism
  • DNA Methylation*
  • DNA-Binding Proteins / metabolism*
  • Dioxygenases
  • Genes, Reporter
  • Genetic Loci
  • Genome, Human
  • HEK293 Cells
  • Humans
  • Mice
  • Plasmids / metabolism
  • Proto-Oncogene Proteins / metabolism*
  • Transfection
  • Uracil / metabolism
  • Uracil-DNA Glycosidase / deficiency
  • Uracil-DNA Glycosidase / metabolism*
  • Zygote / metabolism

Substances

  • 5-carboxylcytosine
  • DNA-Binding Proteins
  • Proto-Oncogene Proteins
  • Uracil
  • Cytosine
  • DNA
  • Dioxygenases
  • Tet2 protein, mouse
  • Uracil-DNA Glycosidase