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

doi:10.7554/eLife.61964

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Article

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

eLife - 19 Nov 2020

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

Abstract excerpt

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...

Topics

Animals
Baculoviridae
Catalytic Domain
Cell Line
Cryoelectron Microscopy
Drosophila Proteins
Drosophila melanogaster
Gene Expression Regulation
Histone-Lysine N-Methyltransferase
Histones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Humans

Methylation

Models, Molecular

Mutation

Protein Conformation

Protein Processing, Post-Translational

Xenopus

Source

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Identifiers

PMID: 33211010
DOI: 10.7554/eLife.61964
PMCID: PMC7725500

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-33211010-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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