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. 2023 Nov 1;129(12):2014–2024. doi: 10.1038/s41416-023-02476-8

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© The Author(s) 2023

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 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/.

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Fig. 2 — a In vitro binding of biotin-tagged H2B 10-amino acid peptide (H2BWTpep) and H2BMUT1pep (mutation of key amino acid) with COMMD4. Beads only lane is the negative control. b A COMMD4 pull-down demonstrating that pre-incubation with the 10-amino acid H2B peptide (H2BWTpep) inhibits the COMMD4-H2B interaction, while pre-incubation with the mutant peptide (H2BMUT1pep) which does not bind to COMMD4, maintains the COMMD4-H2B interaction. INPUT shows the loading. c Binding of overexpressed H2BWTpep (FLAG-H2BWT) and H2BMUT1pep (FLAG-H2BMUT1) with GST-COMMD4. FLAG-H2BWT and FLAG-H2BMUT1 were immunoprecipitated from HEK293T cells and the co-eluting proteins were immunoblotted with antibodies against GST-COMMD4 and FLAG. IgG heavy chain shows the loading.