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. 2017 Nov 6;8:1333. doi: 10.1038/s41467-017-01080-8

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© The Author(s) 2017

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. 7 — Association of XPC with nucleosomes containing H3K4me3. a Interaction of XPC protein with core particles generated by MNase digestion of chromatin. These core particles were immunoprecipitated with anti-H3 or anti-H3K4me3 antibodies and analyzed by immunoblotting; –Ig, immunoglobulins omitted (core particles from UV-irradiated cells subjected to the same procedure except that antibodies were left out). b Quantification of XPC associating with core particles precipitated with anti-H3 or anti-H3K4me3 antibodies. The UV dose was 10 J m^–2; error bars show s.e.m, (n = 3, one-sample t-test with a hypothetical value of 100). c Interaction of XPC protein with histone octamers generated by MNase and benzonase digestion of chromatin. These octamers were immunoprecipitated with anti-H3K4me3 antibodies and analyzed by immunoblotting; –Ig, immunoglobulins omitted. Histones were stained with the Ponceau dye. d Quantification of XPC associating with histone octamers precipitated with anti-H3K4me3 antibodies (n = 3, one-sample t-test). XPC levels in the unirradiated controls are set to 100%. e Histone octamers obtained by MNase and benzonase digestion of chromatin were immunoprecipitated with anti-XPC antibodies; –Ig, immunoglobulins omitted. f Interaction between recombinant XPC and H3K4me3. Lysates from sf9 cells expressing XPC protein were supplemented with H3K4me3 (2 µg) as indicated and immunoprecipitated using anti-H3K4me3 antibodies