Ontology highlight
ABSTRACT:
SUBMITTER: Messner S
PROVIDER: S-EPMC2965223 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Nucleic acids research 20100604 19
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 ...[more]