PARP1 ADP-ribosylates lysine residues of the core histone tails

@inproceedings{Messner2010PARP1AL,
  title={PARP1 ADP-ribosylates lysine residues of the core histone tails},
  author={Simon Messner and Matthias Altmeyer and Hongtao Zhao and Andrea Pozivil and Bernd Roschitzki and Peter Max Gehrig and Dorothea Rutishauser and Danzhi Huang and Amedeo Caflisch and Michael O Hottiger},
  booktitle={Nucleic acids research},
  year={2010}
}
The chromatin-associated enzyme PARP1 has previously been suggested to ADP-ribosylate histones, but the specific ADP-ribose acceptor sites have remained enigmatic. Here, we show that PARP1 covalently ADP-ribosylates the amino-terminal histone tails of all core histones. Using biochemical tools and novel electron transfer dissociation mass spectrometric protocols, we identify for the first time K13 of H2A, K30 of H2B, K27 and K37 of H3, as well as K16 of H4 as ADP-ribose acceptor sites. Multiple… CONTINUE READING

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The role of poly(ADP-ribosyl)ation in epigenetic events

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