Evidence map›Paper›PMID 31221974›Full record

ArticleNature communications2019

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 and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
5.1field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 102 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 2 countries.

Andrea FrapportiInstitut Jacques Monod, Université de Paris, CNRS, 75013, Paris, France.ORCID http://orcid.org/0000-0002-4973-596X
Caridad Miró PinaInstitut Jacques Monod, Université de Paris, CNRS, 75013, Paris, France.ORCID http://orcid.org/0000-0001-5654-8073
Olivier ArnaizInstitute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette CEDEX, France.ORCID http://orcid.org/0000-0002-9626-1015
Daniel HolochInstitut Curie, Paris Sciences et Lettres Research University, INSERM, U934, CNRS, UMR3215, Paris, 75005, France.ORCID http://orcid.org/0000-0001-6399-0230
Takayuki KawaguchiInstitut Jacques Monod, Université de Paris, CNRS, 75013, Paris, France.ORCID http://orcid.org/0000-0001-6688-3879
Adeline HumbertInstitut Jacques Monod, Université de Paris, CNRS, 75013, Paris, France.
Evangelia EleftheriouInstitute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette CEDEX, France.
Bérangère LombardInstitut Curie, Paris Sciences et Lettres Research University, Centre de Recherche, Laboratoire de Spectrométrie de Masse Protéomique, 26 rue d'Ulm, 75248, Cedex 05 Paris, France.
Damarys LoewInstitut Curie, Paris Sciences et Lettres Research University, Centre de Recherche, Laboratoire de Spectrométrie de Masse Protéomique, 26 rue d'Ulm, 75248, Cedex 05 Paris, France.ORCID http://orcid.org/0000-0002-9111-8842
Linda SperlingInstitute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette CEDEX, France.ORCID http://orcid.org/0000-0002-7772-4774
Karine GuitotSorbonne Université, Ecole Normale Supérieure, Paris Sciences et Lettres Research University, CNRS, Laboratoire des biomolécules, LBM, 75005, Paris, France.ORCID http://orcid.org/0000-0002-1866-1208
Raphaël MargueronInstitut Curie, Paris Sciences et Lettres Research University, INSERM, U934, CNRS, UMR3215, Paris, 75005, France.
Sandra DuharcourtInstitut Jacques Monod, Université de Paris, CNRS, 75013, Paris, France. sandra.duharcourt@ijm.fr.ORCID http://orcid.org/0000-0002-8913-8799
Centre National de la Recherche Scientifique · FRUniversité Paris-Sud · FRProtéomique, Réponse Inflammatoire et Spectrométrie de Masse · FR

Funding

Agence Nationale de la Recherche (French National Research Agency) ANR-10-INSB-04Agence Nationale de la Recherche (French National Research Agency) ANR-11-IDEX-0005-02Agence Nationale de la Recherche (French National Research Agency) ANR-11-LABX-0071_WHOAMIAgence Nationale de la Recherche (French National Research Agency) ANR-14-CE10-0005-04 'PIGGYPACK'
6 · The paper itself

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.

Indexed as

Gene SilencingDNA MethylationDNA Transposable ElementsHistonesParamecium tetraureliaPolycomb Repressive Complex 2Protein Processing, Post-TranslationalTranscriptional ActivationDNA Transposable ElementsHistonesPolycomb Repressive Complex 2

Identifiers

PMID31221974
PMCPMC6586856
OpenAlexW2950012758

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.