title: ADP-ribosylation of histones by ARTD1: an additional module of the histone code?
abstract: ADP-ribosylation is a covalent post-translational protein modification catalyzed by ADP-ribosyltransferases and is involved in important processes such as cell cycle regulation, DNA damage response, replication or transcription. Histones are ADP-ribosylated by ADP-ribosyltransferase diphtheria toxin-like 1 at specific amino acid residues, in particular lysines, of the histones tails. Specific ADP-ribosyl hydrolases and poly-ADP-ribose glucohydrolases degrade the ADP-ribose polymers. The ADP-ribose modification is read by zinc finger motifs or macrodomains, which then regulate chromatin structure and transcription. Thus, histone ADP-ribosylation may be considered an additional component of the histone code.
authors.affiliation: Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Zurich, Switzerland. hottiger@vetbio.uzh.ch
authors.forename: Michael O
authors.initials: MO
authors.lastname: Hottiger
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism*; D000818:Animals; D042421:Histone Code; D006657:Histones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012266:Ribose / Q000378:metabolism
chemical_list: D006657:Histones; D000244:Adenosine Diphosphate; D012266:Ribose; D011065:Poly(ADP-ribose) Polymerases