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. 2019 Aug 1;33(15-16):903–935. doi: 10.1101/gad.325050.119

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© 2019 Yu 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. — Biochemical characterization of PRC2 accessory factors. (A) Domains within PRC2 accessory proteins are indicated. SUZ12 binding domains are highlighted by gray dots. (Bottom) Sequence alignment of the Tudor domains within three mammalian PCL proteins. The critical aromatic residues that can form a cage are highlighted by red squares. The cage within the PCL_tudor are bound to H3K36me3 (and, to a lesser extent, H3K36me2) in vitro. (B) PRC2 accessory proteins regulate its activity through several means: increasing its affinity for nucleosome binding (e.g., AEBP2_{KR motif} and JARID2_JmjN) and DNA (e.g., AEBP2_Zn, JARID2_C-term, and PCL_EH), interacting with histone posttranslational modifications (hPTMs) (e.g., JARID2_UIM [H2AK119ub] and PCL_Tudor [H3K36me2/me3]), and/or regulating its allosteric activation (e.g., JARID2-K116me3). (C2B) C2-binding domain; (TR) transrepression; (RBR) RNA-binding region; (JmjN) Jumonji N; (JmjC) Jumonji C; (PHD1/2): plant homeodomain 1/2.