JMJ24 targets CHROMOMETHYLASE3 for proteasomal degradation in Arabidopsis

Genes Dev. 2016 Feb 1;30(3):251-6. doi: 10.1101/gad.274647.115. Epub 2016 Jan 21.

Abstract

H3K9 methylation is usually associated with DNA methylation, and together they symbolize transcriptionally silenced heterochromatin. A number of proteins involved in epigenetic processes have been characterized. However, how the stability of these proteins is regulated at the post-translational level is largely unknown. Here, we show that an Arabidopsis JmjC domain protein, JMJ24, possesses ubiquitin E3 ligase activity. JMJ24 directly targets a DNA methyltransferase, CHROMOMETHYLASE 3 (CMT3), for proteasomal degradation to initiate destabilization of the heterochromatic state of endogenous silenced loci. Our results uncover an additional connection between two conserved epigenetic modifications: histone modification and DNA methylation.

Keywords: CMT3; E3 ligase; JmjC protein; histone demethylation; protein stability; transcriptional gene silencing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / enzymology*
  • Arabidopsis / genetics
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • DNA-Cytosine Methylases / genetics
  • DNA-Cytosine Methylases / metabolism
  • Epigenesis, Genetic
  • Jumonji Domain-Containing Histone Demethylases / metabolism*
  • Methylation
  • Proteasome Endopeptidase Complex / genetics
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Stability
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitination

Substances

  • Arabidopsis Proteins
  • JMJ24 protein, Arabidopsis
  • Jumonji Domain-Containing Histone Demethylases
  • DNA-Cytosine Methylases
  • CMT3 protein, Arabidopsis
  • Ubiquitin-Protein Ligases
  • Proteasome Endopeptidase Complex