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. 2010 Jun 4;38(19):6350–6362. doi: 10.1093/nar/gkq463

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — ADP-ribosylation of the H4 peptide is impaired by H4K16 acetylation. (A) Elution profile of biotinylated H4 peptide (aa 1–22) and biotinylated H4K16ac peptide (aa 1–22) incubated with 100 μM NAD⁺ for 15 min without PARP1 (–PARP1) or in the presence of PARP1 (+PARP1) and subsequent ARH3 treatment. Acetone precipitated peptides were analyzed by LC–MS/MS using a C18 reversed-phase column and subsequent detection by mass spectrometry. (B) Histone H4 (aa 1–22) and acetylated H4K16ac (1–22) peptides were ADP-ribosylated with PARP1 for 15 min at 30°C with 100 nM ³²P-NAD⁺. The peptides were purified by microvolume-C18 reversed phase columns, eluted into scintillation liquid and counted for incorporated ³²P. Relative increase of counts per minutes was calculated over background (peptides added after termination of the reaction by 3AB). (C) Overview of the identified ADP-ribose acceptor sites within the amino-terminal core histone tails.