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. 2019 Jan 3;10:36. doi: 10.1038/s41467-018-07906-3

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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. 3 — Interaction between ePHD₆ of MLL3/4 and histone H4 is required for their nucleosomal methylation activity. a Schematic representation of constructs used in the histone methyltransferase (HMT) assay. Stars indicate the mutations in PHD₆ of MLL3/MLL4. 1 M is W1109A single point mutation of MLL3, 2 M: W1109A/E1120A and W1529A/E1540A are double point mutations of MLL3 and corresponding residues in MLL4, respectively, MLL4 fusion-4M is a quadruple point mutant (E1516A/E1517A/D1518A/E1544A) of MLL4, and E1517 of MLL4 corresponds to E1097 of MLL3. b, c Comparison of HMT activities of different MLL3/MLL4 constructs. d, e Effects of different histone H4 mutants on HMT activities of MLL3_PHD_4-6-C and MLL4 fusion proteins