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. 2020 Dec 4;11:6212. doi: 10.1038/s41467-020-20089-0

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© The Author(s) 2020

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 8 — When BPC is present, AIPP3-BAH, and AIPP2/PAIPP2-PHD motifs recognize H3K27me3, which is deposited by PRC2 complex, and unmodified H3K4 around the TSS, respectively. Then, the BAH–PHD histone reader module recruit CPL2 to dephosphorylate Pol II at the fifth Ser of CTD, thereby repressing the transcriptional initiation and subsequent elongation of Pol II. When BPC is absent, active H3K4me3 mark is deposited. Pol II CTD-Ser2 and -Ser5 residues can be phosphorylated sequentially, leading to release of Pol II from initiation to elongation state.