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

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

H3K9me3 and H3K27me3 chromatin silencing marks are usually deposited by different SET-domain proteins. Here the authors show that the Enhancer-of-zeste-like protein Ezl1, from the unicellular eukaryote Paramecium tetraurelia, catalyzes methylation of histone H3 in vitro and in vivo with an apparent...

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Autores principales: 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, Sandra Duharcourt
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/a486884fd7c44e3eb795b8444d15483e
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spelling oai:doaj.org-article:a486884fd7c44e3eb795b8444d15483e2021-12-02T16:57:21ZThe Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium10.1038/s41467-019-10648-52041-1723https://doaj.org/article/a486884fd7c44e3eb795b8444d15483e2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10648-5https://doaj.org/toc/2041-1723H3K9me3 and H3K27me3 chromatin silencing marks are usually deposited by different SET-domain proteins. Here the authors show that the Enhancer-of-zeste-like protein Ezl1, from the unicellular eukaryote Paramecium tetraurelia, catalyzes methylation of histone H3 in vitro and in vivo with an apparent specificity toward K9 and K27, and controls the repression of transposable elements.Andrea FrapportiCaridad Miró PinaOlivier ArnaizDaniel HolochTakayuki KawaguchiAdeline HumbertEvangelia EleftheriouBérangère LombardDamarys LoewLinda SperlingKarine GuitotRaphaël MargueronSandra DuharcourtNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
Sandra Duharcourt
The Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium
description H3K9me3 and H3K27me3 chromatin silencing marks are usually deposited by different SET-domain proteins. Here the authors show that the Enhancer-of-zeste-like protein Ezl1, from the unicellular eukaryote Paramecium tetraurelia, catalyzes methylation of histone H3 in vitro and in vivo with an apparent specificity toward K9 and K27, and controls the repression of transposable elements.
format article
author 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
Sandra Duharcourt
author_facet 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
Sandra Duharcourt
author_sort Andrea Frapporti
title The Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium
title_short The Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium
title_full The Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium
title_fullStr The Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium
title_full_unstemmed The Polycomb protein Ezl1 mediates H3K9 and H3K27 methylation to repress transposable elements in Paramecium
title_sort polycomb protein ezl1 mediates h3k9 and h3k27 methylation to repress transposable elements in paramecium
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/a486884fd7c44e3eb795b8444d15483e
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