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

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

doi:10.7554/eLife.61964

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

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Finogenova, Ksenia
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons243828

Bonnet, Jacques
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons244738

Schäfer, Ingmar B.
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons181439

Finkl, Katja
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons221688

Schmid, Katharina
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons256154

Litz, Claudia
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons137910

Strauss, Mike
Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77736

Benda, Christian
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Müller, Jürg
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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elife-61964-figures-v3.pdf
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Citation

Finogenova, K., Bonnet, J., Poepsel, S., Schäfer, I. B., Finkl, K., Schmid, K., et al. (2020). Structural basis for PRC2 decoding of active histone methylation marks H3K36me2/3. eLife, 9: e61964. doi:10.7554/eLife.61964.

Cite as: https://hdl.handle.net/21.11116/0000-0007-D3E6-7

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 in vitro. Accordingly, Drosophila H3K36A and H3K36R mutants show reduced levels of H3K27me3 and defective Polycomb repression of HOX genes. The relay of interactions between EZH2, the nucleosomal DNA and the H3 N-terminus therefore creates the geometry that permits allosteric inhibition of PRC2 by methylated H3K36 in transcriptionally active chromatin.