PARP1 ADP-ribosylates lysine residues of the core histone tails

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 n...

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Detalles Bibliográficos
Autores principales: Messner, Simon, Altmeyer, Matthias, Zhao, Hongtao, Pozivil, Andrea, Roschitzki, Bernd, Gehrig, Peter, Rutishauser, Dorothea, Huang, Danzhi, Caflisch, Amedeo, Hottiger, Michael O.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2010
Materias:
Gene Regulation, Chromatin and Epigenetics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2965223/
https://www.ncbi.nlm.nih.gov/pubmed/20525793
http://dx.doi.org/10.1093/nar/gkq463

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2965223/
https://www.ncbi.nlm.nih.gov/pubmed/20525793
http://dx.doi.org/10.1093/nar/gkq463

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