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The Paramecium Ezl1 protein mediates dual methylation of H3 lysines 9 and 27

ABSTRACT: The goal of the present project was to determine which Paramecium histone H3 residues are methylated in an Ezl1-dependent manner.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Paramecium Tetraurelia

SUBMITTER: Guillaume Arras

LAB HEAD: Damarys Loew

PROVIDER: PXD012170 | Pride | 2019-06-26

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	F032344.dat	Other
	F032344.mzid.gz	Mzid
	F032344.pride.mztab.gz	Mztab
	F032345.dat	Other
	F032345.mzid.gz	Mzid

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Publications

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

Frapporti Andrea A Miró Pina Caridad C Arnaiz Olivier O Holoch Daniel D Kawaguchi Takayuki T Humbert Adeline A Eleftheriou Evangelia E Lombard Bérangère B Loew Damarys D Sperling Linda L Guitot Karine K Margueron Raphaël R Duharcourt Sandra S

Nature communications 20190620 1

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 similar ...[more]

PMID: 31221974

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