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Reversible mono‐ADP‐ribosylation of DNA breaks

The FEBS journal, 2017-12, Vol.284 (23), p.4002-4016 [Peer Reviewed Journal]

2017 The Authors. published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. ;2017 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. ;Copyright © 2017 Federation of European Biochemical Societies ;ISSN: 1742-464X ;EISSN: 1742-4658 ;DOI: 10.1111/febs.14297 ;PMID: 29054115

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Title:
Reversible mono‐ADP‐ribosylation of DNA breaks
Author: Munnur, Deeksha ; Ahel, Ivan
Subjects: Adducts ; Adenine ; Adenosine ; Adenosine diphosphate ; Adenosine Diphosphate Ribose - metabolism ; ADP-Ribosylation ; ADP‐ribose hydrolase ; Animals ; Apoptosis ; Bacteria ; Biological activity ; Cell Cycle Proteins - metabolism ; Chemical modification ; Chromatin remodeling ; Deoxyribonucleic acid ; DNA ; DNA - genetics ; DNA - metabolism ; DNA adducts ; DNA Breaks ; DNA damage ; DNA Repair ; Editor's Choice ; Humans ; Hydrolases - metabolism ; Macromolecules ; Metabolism ; Models, Genetic ; NAD ; NAD - metabolism ; NADPH ; Nicotinamide ; Nicotinamide adenine dinucleotide ; PARP ; Phosphates ; Poly(ADP-ribose) Polymerases - metabolism ; Polymers ; Proteins ; Ribose ; Ribosylation ; Transcription
Is Part Of: The FEBS journal, 2017-12, Vol.284 (23), p.4002-4016
Description: Adenosine diphosphate (ADP)‐ribosylation is a chemical modification of macromolecules that plays an important role in regulation of quintessential biological processes such as DNA repair, transcription, chromatin remodelling, stress response, apoptosis, bacterial metabolism and many others. ADP‐ribosylation is carried out by ADP‐ribosyltransferase proteins, such as poly (ADP‐ribose) polymerases (PARPs) that transfer either monomer or polymers of ADP‐ribose onto the molecular targets by using nicotinamide adenine dinucleotide (NAD+) as a cofactor. Traditionally, proteins have been described as primary targets of ADP‐ribosylation; however, there has been growing evidence that DNA may be a common target as well. Here, we show using biochemical studies that PARP3, a DNA damage‐activated ADP‐ribosyltransferase, can mono‐ADP‐ribosylate double‐stranded DNA ends. ADP‐ribosylation of DNA mediated by PARP3 attaches a single mono‐ADP‐ribose moiety to the phosphate group at the terminal ends of DNA. We further show that mono ADP‐ribosylation at DNA ends can be efficiently reversed by several cellular hydrolases (PARG, MACROD2, TARG1 and ARH3). This suggests that mono ADP‐ribosylated DNA adducts can be efficiently removed in cells by several mechanisms. The addition of adenosine diphosphate (ADP)‐ribose to macromolecules regulates important biological processes including DNA repair, transcription, cell signalling and apoptosis. ADP‐ribosylation is catalysed by poly (ADP‐ribose) polymerases (PARPs), which add monomers or polymers of ADP‐ribose to target molecules. Although PARPs are generally thought to target proteins, PARP1 and PARP2 can also add polymers of ADP‐ribose to DNA ends in vitro. Munnur and Ahel now report that PARP3 covalently attaches a mono‐ADP‐ribose unit to the terminal phosphate group at the 5′ end of DNA. Intriguingly, this modification can be removed by poly (ADP‐ribose) glycohydrolase (PARG), suggesting that mono‐ADP‐ribosylation might have an important role in DNA repair.
Publisher: England: Blackwell Publishing Ltd
Language: English
Identifier: ISSN: 1742-464X
EISSN: 1742-4658
DOI: 10.1111/febs.14297
PMID: 29054115
Source: Geneva Foundation Free Medical Journals at publisher websites
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Reversible mono‐ADP‐ribosylation of DNA breaks

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