Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 4, Pages 508-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2523
Keywords
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Funding
- EMBL
- Ludwig Maximilians University of Munich
- EU FP7 Marie Curie Initial Training Network Nucleosome4D
- Deutsche Forschungsgemeinschaft [LA 2489/1-1]
- Center for Integrated Protein Science Munich
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ADP-ribosylation is a reversible post-translational modification with wide-ranging biological functions in all kingdoms of life. A variety of enzymes use NAD(+) to transfer either single or multiple ADP-ribose (ADPr) moieties onto distinct amino acid substrates, often in response to DNA damage or other stresses. Poly-ADPr-glycohydrolase readily reverses poly-ADP-ribosylation induced by the DNA-damage sensor PARP1 and other enzymes, but it does not remove the most proximal ADPr linked to the target amino acid. Searches for enzymes capable of fully reversing cellular mono-ADP-ribosylation back to the unmodified state have proved elusive, which leaves a gap in the understanding of this modification. Here, we identify a family of macrodomain enzymes present in viruses, yeast and animals that reverse cellular ADP-ribosylation by acting on mono-ADP-ribosylated substrates. Our discoveries establish the complete reversibility of PARP-catalyzed cellular ADP-ribosylation as a regulatory modification.
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