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. 2019 Oct 17;10:4724. doi: 10.1038/s41467-019-12551-5

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© The Author(s) 2019

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. 1 — The native MORF complex is a H3K23-specific HAT. a A diagram of MORF with the MORF_N region indicated. b The MORF complex subunit composition. c Purified native MOZ and MORF complexes from K562 cells shown by silver staining. d Confirmation of the subunits of the native purified MORF complex by Western blots using specific antibodies. Source data are provided as a Source Data file. e HAT activity of native MORF complex from K562 cells on the indicated H3 peptides. Liquid HAT assays, in which reactions were spotted on P81 filters and counted by scintillation as counts per minute (CPM). f HAT activity of the MORF_N complex overexpressed in 293T cells on indicated H3 peptides. g Cartoon showing interrelated activities of the adjacent DPF and MYST domains. The MYST domain acetylates primarily H3K23 and has some HAT activity on H3K14, whereas MORF_DPF binds to unmodified H3 or acylated H3K14, preferring H3K14cr (see below). Error bars indicate the range from duplicate samples, n = 2 independent experiments