Evidence map›Paper›PMID 29058709›Full record

ArticleNature structural & molecular biology2017

Molecular analysis of PRC2 recruitment to DNA in chromatin and its inhibition by RNA.

Xueyin Wang, Richard D Paucek, Anne R Gooding, Zachary Z Brown, Eva J Ge, Tom W Muir, Thomas R Cech

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed, 1 pooled it
11.6field-weighted citation impact, top 1% 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

148 citing papers in PubMed, 1 synthesis or guideline pooled it, 226 citations in OpenAlex.

  1. Pooled it
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  7. Phosphorylation event changes the RNA binding mode of EZH2 disordered segment.Protein science : a publication of the Protein Society · 2026
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88 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

7 authors at 2 institutions in 1 country.

Xueyin WangDepartment of Chemistry & Biochemistry, BioFrontiers Institute, University of Colorado Boulder, Boulder, Colorado, USA.
Richard D PaucekDepartment of Chemistry & Biochemistry, BioFrontiers Institute, University of Colorado Boulder, Boulder, Colorado, USA.ORCID http://orcid.org/0000-0002-4105-2443
Anne R GoodingDepartment of Chemistry & Biochemistry, BioFrontiers Institute, University of Colorado Boulder, Boulder, Colorado, USA.
Zachary Z BrownDepartment of Chemistry, Princeton University, Princeton, New Jersey, USA.
Eva J GeDepartment of Chemistry, Princeton University, Princeton, New Jersey, USA.
Tom W MuirDepartment of Chemistry, Princeton University, Princeton, New Jersey, USA.
Thomas R CechDepartment of Chemistry & Biochemistry, BioFrontiers Institute, University of Colorado Boulder, Boulder, Colorado, USA.ORCID http://orcid.org/0000-0001-7338-3389
Howard Hughes Medical Institute · USPrinceton University · US

Funding

Shared Resources Core 2: Quantitative Proteomics CoreP01CA196539 · NCI · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2015 to 2024
$17.6M
Structure, Function and Applications of InteinsR37GM086868 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2012 to 2021
$5.4M
Structure, Function and Applications of InteinsR01GM086868 · NIGMS · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2008 to 2025
$4.4M
Howard Hughes Medical InstituteNCI NIH HHS P01 CA196539NIGMS NIH HHS R01 GM086868NIGMS NIH HHS R37 GM086868
6 · The paper itself

Abstract

Many studies have revealed pathways of epigenetic gene silencing by Polycomb repressive complex 2 (PRC2) in vivo, but understanding the underlying molecular mechanisms requires biochemistry. Here we analyze interactions of reconstituted human PRC2 with nucleosome complexes. Histone modifications, the H3K27M cancer mutation, and inclusion of JARID2 or EZH1 in the PRC2 complex have unexpectedly minor effects on PRC2-nucleosome binding. Instead, protein-free linker DNA dominates the PRC2-nucleosome interaction. Specificity for CG-rich sequences is consistent with PRC2 occupying CG-rich DNA in vivo. PRC2 preferentially binds methylated DNA regulated by its AEBP2 subunit, suggesting how DNA and histone methylation collaborate to repress chromatin. We find that RNA, known to inhibit PRC2 activity, is not a methyltransferase inhibitor per se. Instead, RNA sequesters PRC2 from nucleosome substrates, because PRC2 binding requires linker DNA, and RNA and DNA binding are mutually exclusive. Together, we provide a model for PRC2 recruitment and an explanation for how actively transcribed genomic regions bind PRC2 but escape silencing.

Indexed as

Base CompositionCell LineChromatinDNADNA-Binding ProteinsDNA MethylationEpigenesis, GeneticGene SilencingHistonesHumansNucleosomesPolycomb Repressive Complex 2Protein BindingRepressor ProteinsRNAAEBP2 protein, humanChromatinDNADNA-Binding ProteinsEZH1 protein, humanHistonesJARID2 protein, humanMTF2 protein, humanNucleosomesPolycomb Repressive Complex 2Repressor ProteinsRNA

Identifiers

PMID29058709
PMCPMC5771497
OpenAlexW2765753520

What OpenQuestion holds

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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.