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ADP‐ribosylation of histones by ARTD1: An additional module of the histone code?
Author(s) -
Hottiger Michael O.
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.03.031
Subject(s) - adp ribosylation , histone , histone h1 , chromatin , histone modifying enzymes , histone code , histone h2a , biochemistry , histone h2b , histone octamer , microbiology and biotechnology , chemistry , biology , dna , nucleosome , enzyme , nad+ kinase
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.

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