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ADP-ribosylation of histones by ARTD1: An additional module of the histone code?

期刊

FEBS LETTERS
卷 585, 期 11, 页码 1595-1599

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.03.031

关键词

ADP-ribosylation; ARTD1 (PARP-1); Chromatin; Epigenetic; Histone code; Posttranslational modification

资金

  1. SNF [31-122421]
  2. Kanton of Zurich

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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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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