title: Histone ADP-ribosylation in DNA repair, replication and transcription.
abstract: 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.
authors: Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
authors: Simon
authors: S
authors: Messner
authors: Michael O
authors: MO
authors: Hottiger
mesh_terms: D036002:ADP Ribose Transferases / Q000378:metabolism; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D002453:Cell Cycle; D002843:Chromatin / Q000378:metabolism; D042002:Chromatin Assembly and Disassembly; D004260:DNA Repair; D004261:DNA Replication; D006657:Histones / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D014158:Transcription, Genetic
chemical_list: D002843:Chromatin; D006657:Histones; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases