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. 2022 Aug 27;14:107. doi: 10.1186/s13148-022-01323-6

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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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 15 — The linkage between DNA methylation and histone modification in pluripotency genes. In embryonic stem cells, pluripotency genes such as Oct 3/4 and Nanog have acetylated (unmethylated) CpG islands. These islands are combined with acetylated Histones (Ac) H3 and H4 and methylated (Me) lysine 4(K4) of Histone H3. With the initiation of differentiation histone methyltransferase (G9a) together with histone deacetylase (HDAc) enzyme binds to the complex. The binding leads to deacetylation of H3 and H4. At the same time demethylation of K4 is catalyzed by HDAc and methylation of K9 is catalyzed by G9a. This modification created a binding site for the chromodomain protein heterochromatin protein 1(HP1). Finally, G9a recruits the methylases DNMT3A and DNMT3B (dark purple circles), which will mediate the de novo methylation of the deacetylated DNA [232, 234]. The process favors epigenetic silencing and methylation while blocking heterochromatinization. Image reprinted from [235] with permission of the publisher (Request ID 600061575 25 Nov 2021)