Journal
TRENDS IN CELL BIOLOGY
Volume 21, Issue 9, Pages 534-542Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2011.06.001
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Funding
- Swiss National Science Foundation [31-122421]
- Kanton of Zurich
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Most published work on post-translational histone modifications focuses on small covalent alterations such as acetylation, methylation and phosphorylation. By contrast, fewer data are available on the modification of histones by ADP-ribose. Discussion of the biological significance of histone ADP-ribosylation has often been restricted to functions of the modifying enzymes, rather than to histones as ADP-ribose acceptors. In particular, the identification of specific lysine residues as ADP-ribose acceptor sites in histones and the identification of ADP-ribose binding modules raise this modification to a par with acetylation, methylation or phosphorylation. We discuss here the functional aspects of histone ADP-ribosylation and its influence on DNA repair, replication and transcription.
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