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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. 8 — A Schematic representation of the PARG domain architecture. The catalytic domain is composed of two subdomains; an accessory domain (AD, yellow) and macrodomain (macro, red). Domain boundaries are given below and the catalytic EE motif (black line) above the diagram. Abbreviation C. elegans PARG1, cPARG1; D. melanogaster Parg, dParg; Homo sapiens PARG, hPARG; Tetrahymena thermophila Parg, tParg. B Activity of dParg catalytic mutants and C-terminal truncations on poly-Glu-automodified hPARP1. Poly-Glu-automodified hPARP1 was obtained as described in Fig. 6C and subsequently supplemented with dParg WT or with indicated mutants. The experiment was repeated independently three times with similar results. C Activity of dParg catalytic mutants and C-terminal truncations on purified mono-Ser-ADP-ribosylated histone H3 peptide (aa 1–21). Mono-Ser-ADP-ribosylated histone H3 peptide (aa 1–21) was obtained as described in Methods and subsequently supplemented with dParg WT or with indicated mutants. The experiment was repeated independently three times with similar results.