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. 2023 Jun 2;14:3200. doi: 10.1038/s41467-023-38793-y

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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 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 — A Removal of poly-Ser-ADPr on automodified hPARP1 in the presence of hHPF1 and poly-Ser-ADP-ribosylated histone H3/H4 tetramer by human and Drosophila (ADP-ribosyl)hydrolases. The reaction was performed as in Fig. 5A, except histone H3/H4 tetramer was used instead of histone H3 peptide. Lower panel shows CBB stained SDS-PAGE of the proteins. The experiment was repeated independently three times with similar results. B Removal of poly-ADPr on automodified hPARP1 (0.5 μM), in the presence of hHPF1 (0.5 μM) and mono-Ser-ADP-ribosylated H3 peptide (aa 1–21, 0.5 µg) by human and Drosophila (ADP-ribosyl)hydrolases. Reactions were performed as described in Fig. 5A. Lower panel shows the CBB stained SDS-PAGE of the proteins. The experiment was repeated independently three times with similar results. C Removal of mono-Ser-ADPr on mono-Ser-ADP-ribosylated histone H3 peptide (aa 1–21) by human and Drosophila (ADP-ribosyl)hydrolases. Reactions were performed as described in Fig. 1A and peptide purified as described in Fig. 1B. Lower panel shows CBB stained SDS-PAGE of the proteins. The experiment was repeated independently three times with similar results. D Measurements of hydrolase activity of indicated hydrolases against synthetic histone H2B peptide mono-Ser-ADPr on S7 using the AMP-Glo assay (Promega). Samples are background corrected and normalised to hARH3. Data represent triplicate measurements of three independent experiments ± SEM.