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. 2019 Oct 1;33(19-20):1428–1440. doi: 10.1101/gad.328773.119

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© 2019 Lee et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 5. — The level of EZH2 automethylation remains intact upon loss of allosteric activation. (A) A schematic illustration of EZH2 and EED structures, including an H3K27me3 peptide that interacts with the aromatic cage of EED as an allosteric stimulator and an H3 tail peptide present in the SET domain of EZH2 as substrate. Allosteric mutations in the EED cage (EED Y365A; pink dot), EED/EZH2-SRM interface (EED R302G; yellow dot), and SRM domain of EZH2 [P132S (turquoise dot) and F145L (blue dot)] are indicated. (B,C) EZH2 automethylation requires EED but occurs independently from allosteric activation of PRC2. Western blot analyses of EZH2-K514me3, EZH2, EED, GAPDH, H3K27me2, H3K27me3, and total histone H3 levels in E14 mESCs, either WT or EED-KO, and in B6 mESCs, either WT or EZH1/2 dKO with or without EZH2 rescue conditions. mESC, mouse embryonic stem cells. Asterisks indicate nonspecific bands.