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Significance A subset of deadly pediatric brain tumors called diffuse intrinsic pontine gliomas express a mutant histone H3 with a lysine-to-methionine substitution at position 27 (H3K27M), which has been shown to drive tumorigenesis in these cancers. While there is evidence that H3K27M inhibits the H3K27 methyltransferase known as polycomb repressive complex 2 (PRC2), the precise mechanisms by which H3K27M acts remain a matter of debate. In this work, we used biochemical and in cell assays to characterize the dependence of PRC2 binding to H3K27M on other PRC2 ligands, including H3K27me3. We synthesized designer chromatin inhibitors containing H3K27M and H3K27me3 nucleosomes and found that PRC2 is inhibited by a dinucleosome, suggesting that PRC2 is sequestered on chromatin by these bivalent inhibitors.

PRC2 engages a bivalent H3K27M-H3K27me3 dinucleosome inhibitor