The Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2019

The Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium

Andrea Frapporti
  • Fonction : Auteur
Caridad Miró Pina
  • Fonction : Auteur
Daniel Holoch
Takayuki Kawaguchi
Adeline Humbert
  • Fonction : Auteur
Evangelia Eleftheriou
  • Fonction : Auteur
Bérangère Lombard
  • Fonction : Auteur
Damarys Loew
Karine Guitot
  • Fonction : Auteur
Raphaël Margueron
  • Fonction : Auteur
Sandra Duharcourt

Résumé

In animals and plants, the H3K9me3 and H3K27me3 chromatin silencing marks are deposited by different protein machineries. H3K9me3 is catalyzed by the SET-domain SU(VAR)3-9 enzymes, while H3K27me3 is catalyzed by the SET-domain Enhancer-of-zeste enzymes, which are the catalytic subunits of Polycomb Repressive Complex 2 (PRC2). Here, we show that the Enhancer-of-zeste-like protein Ezl1 from the unicellular eukaryote Paramecium tetraurelia, which exhibits significant sequence and structural similarities with human EZH2, catalyzes methylation of histone H3 in vitro and in vivo with an apparent specificity toward K9 and K27. We find that H3K9me3 and H3K27me3 co-occur at multiple families of transposable elements in an Ezl1-dependent manner. We demonstrate that loss of these histone marks results in global transcriptional hyperactivation of transposable elements with modest effects on protein-coding gene expression. Our study suggests that although often considered functionally distinct, H3K9me3 and H3K27me3 may share a common evolutionary history as well as a common ancestral role in silencing transposable elements.

Dates et versions

hal-02164121 , version 1 (24-06-2019)

Identifiants

Citer

Andrea Frapporti, Caridad Miró Pina, Olivier Arnaiz, Daniel Holoch, Takayuki Kawaguchi, et al.. The Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium. Nature Communications, 2019, 10 (1), pp.2710. ⟨10.1038/s41467-019-10648-5⟩. ⟨hal-02164121⟩
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