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. 2022 Sep 7;144(5):1027–1048. doi: 10.1007/s00401-022-02489-2

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© The Author(s) 2022

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — BioID interactome of wild-type and mutant H3. A Summary of high-confidence interactors detected with each histone. B Heatmap of all peptide counts of all high-confidence interactors identified in the experiment. C Heatmap depicting proteins differentially bound by any oncohistone relative to its WT control. D Bubble plot showing differential enrichment of PRC2 components with each oncohistone relative to its WT control. Size = log2(mutant/WT). Color represents significance. Statistically significant (p < 0.05) differential interactions have a black border. E Network of Reactome and KEGG pathways significantly enriched (p < 0.05) among differentially bound proteins by each oncohistone. Node size and color reflects significance and edge thickness reflects number of proteins shared between two nodes. F Heatmap of relative peptide counts of proteins with direct histone modifying activity identified by BioID. Average peptides per histone were Z-transformed