Evidence map›Paper›PMID 33211010›Full record

ArticleeLife2020

Structural basis for PRC2 decoding of active histone methylation marks H3K36me2/3.

Ksenia Finogenova, Jacques Bonnet, Simon Poepsel, Ingmar B Schäfer, Katja Finkl, Katharina Schmid, Claudia Litz, Mike Strauss, Christian Benda, Jürg Müller

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed, 1 pooled it
5.9field-weighted citation impact, top 3% 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

79 citing papers in PubMed, 1 synthesis or guideline pooled it, 124 citations in OpenAlex.

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19 more citing papers are in PubMed but not listed here.

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

10 authors at 2 institutions in 3 countries.

Ksenia FinogenovaMax Planck Institute of Biochemistry, Laboratory of Chromatin Biology, Martinsried, Germany.ORCID https://orcid.org/0000-0002-7512-8637
Jacques BonnetMax Planck Institute of Biochemistry, Laboratory of Chromatin Biology, Martinsried, Germany.
Simon PoepselCalifornia Institute for Quantitative Biology (QB3), University of California, California Institute for Quantitative Biology (QB3), Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, United States.
Ingmar B SchäferMax Planck Institute of Biochemistry, Department of Structural Cell Biology, Martinsried, Germany.
Katja FinklMax Planck Institute of Biochemistry, Laboratory of Chromatin Biology, Martinsried, Germany.
Katharina SchmidMax Planck Institute of Biochemistry, Laboratory of Chromatin Biology, Martinsried, Germany.
Claudia LitzMax Planck Institute of Biochemistry, Laboratory of Chromatin Biology, Martinsried, Germany.
Mike StraussMax Planck Institute of Biochemistry, cryoEM Facility, Martinsried, Germany.
Christian BendaMax Planck Institute of Biochemistry, Department of Structural Cell Biology, Martinsried, Germany.
Jürg MüllerMax Planck Institute of Biochemistry, Laboratory of Chromatin Biology, Martinsried, Germany.ORCID https://orcid.org/0000-0003-2391-4641
Max Planck Institute of Biochemistry · DEQB3 · US

Funding

Deutsche Forschungsgemeinschaft SFB1064
6 · The paper itself

Abstract

Repression of genes by Polycomb requires that PRC2 modifies their chromatin by trimethylating lysine 27 on histone H3 (H3K27me3). At transcriptionally active genes, di- and tri-methylated H3K36 inhibit PRC2. Here, the cryo-EM structure of PRC2 on dinucleosomes reveals how binding of its catalytic subunit EZH2 to nucleosomal DNA orients the H3 N-terminus via an extended network of interactions to place H3K27 into the active site. Unmodified H3K36 occupies a critical position in the EZH2-DNA interface. Mutation of H3K36 to arginine or alanine inhibits H3K27 methylation by PRC2 on nucleosomes

Indexed as

AnimalsBaculoviridaeCatalytic DomainCell LineCryoelectron MicroscopyDrosophila melanogasterDrosophila ProteinsGene Expression RegulationHistone-Lysine N-MethyltransferaseHistonesHumansMethylationModels, MolecularMutationProtein ConformationProtein Processing, Post-TranslationalDrosophila ProteinsHistone-Lysine N-MethyltransferaseHistonesPRC2 protein, Drosophilachromosomescryo-EMD. melanogasterDrosophilagene expressionH3K36me2/3histonehumanmolecular biophysicsnucleosomepolycomb repressive complex 2structural biology

Identifiers

PMID33211010
PMCPMC7725500
OpenAlexW3105996453

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.