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

Andrea Frapporti, Caridad Miró Pina, Olivier Arnaiz, Daniel Holoch, Takayuki Kawaguchi, Adeline Humbert, Evangelia Eleftheriou, Bérangère Lombard, Damarys Loew, Linda Sperling, Karine Guitot, Raphaël Margueron and Sandra Duharcourt ()
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Andrea Frapporti: Institut Jacques Monod, Université de Paris, CNRS
Caridad Miró Pina: Institut Jacques Monod, Université de Paris, CNRS
Olivier Arnaiz: Institute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Univ. Paris-Sud, Université Paris-Saclay
Daniel Holoch: Institut Curie, Paris Sciences et Lettres Research University, INSERM, U934, CNRS, UMR3215
Takayuki Kawaguchi: Institut Jacques Monod, Université de Paris, CNRS
Adeline Humbert: Institut Jacques Monod, Université de Paris, CNRS
Evangelia Eleftheriou: Institute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Univ. Paris-Sud, Université Paris-Saclay
Bérangère Lombard: Institut Curie, Paris Sciences et Lettres Research University, Centre de Recherche, Laboratoire de Spectrométrie de Masse Protéomique
Damarys Loew: Institut Curie, Paris Sciences et Lettres Research University, Centre de Recherche, Laboratoire de Spectrométrie de Masse Protéomique
Linda Sperling: Institute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Univ. Paris-Sud, Université Paris-Saclay
Karine Guitot: Sorbonne Université, Ecole Normale Supérieure, Paris Sciences et Lettres Research University, CNRS, Laboratoire des biomolécules, LBM
Raphaël Margueron: Institut Curie, Paris Sciences et Lettres Research University, INSERM, U934, CNRS, UMR3215
Sandra Duharcourt: Institut Jacques Monod, Université de Paris, CNRS

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-10648-5

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