Apr 23, 2020

Structural basis for decoding active histone methylation marks by Polycomb Repressive Complex 2

BioRxiv : the Preprint Server for Biology
K. FinogenovaJ. Müller

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 trimethylated H3K36 inhibit PRC2. Here, the cryo-EM structure of PRC2 on nucleosomes 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 inhibits H3K27 methylation by PRC2. Accordingly, Drosophila H3K36 mutants show altered H3K27me3 profiles and deregulated expression of HOX genes. The relay of interactions between EZH2, nucleosomal DNA and the H3 N-terminus therefore creates the geometry for allosteric inhibition of PRC2 by methylated H3K36 in transcriptionally active chromatin.

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