Reversible ADP-ribosylation of RNA.
Identifieur interne : 000189 ( PubMed/Checkpoint ); précédent : 000188; suivant : 000190Reversible ADP-ribosylation of RNA.
Auteurs : Deeksha Munnur [Royaume-Uni] ; Edward Bartlett [Royaume-Uni] ; Petra Mikol Evi [Croatie] ; Ilsa T. Kirby [États-Unis] ; Johannes Gregor Matthias Rack [Royaume-Uni] ; Andreja Miko [Croatie] ; Michael S. Cohen [États-Unis] ; Ivan Ahel [Royaume-Uni]Source :
- Nucleic acids research [ 1362-4962 ] ; 2019.
Descripteurs français
- KwdFr :
- ADN simple brin (métabolisme), ADP (), ADP ribose transferases (génétique), ARN (métabolisme), Adénosine diphosphate ribose, Animaux, Catalyse, Chromatine (), Enzymes de réparation de l'ADN (métabolisme), Escherichia coli (métabolisme), Humains, Hydrolases (métabolisme), Maturation post-traductionnelle des protéines, NAD (métabolisme), Phosphorylation, Phosphotransferases (Alcohol Group Acceptor) (), Plasmides (métabolisme), Poly(ADP-ribose) polymerases (métabolisme), Protéines proto-oncogènes (métabolisme), Réparation de l'ADN, Souris, Transduction du signal.
- MESH :
- génétique : ADP ribose transferases.
- métabolisme : ADN simple brin, ARN, Enzymes de réparation de l'ADN, Escherichia coli, Hydrolases, NAD, Plasmides, Poly(ADP-ribose) polymerases, Protéines proto-oncogènes.
- ADP, Adénosine diphosphate ribose, Animaux, Catalyse, Chromatine, Humains, Maturation post-traductionnelle des protéines, Phosphorylation, Phosphotransferases (Alcohol Group Acceptor), Réparation de l'ADN, Souris, Transduction du signal.
English descriptors
- KwdEn :
- ADP Ribose Transferases (genetics), ADP-Ribosylation, Adenosine Diphosphate (chemistry), Adenosine Diphosphate Ribose, Animals, Catalysis, Chromatin (chemistry), DNA Repair, DNA Repair Enzymes (metabolism), DNA, Single-Stranded (metabolism), Escherichia coli (metabolism), Humans, Hydrolases (metabolism), Mice, NAD (metabolism), Phosphorylation, Phosphotransferases (Alcohol Group Acceptor) (chemistry), Plasmids (metabolism), Poly(ADP-ribose) Polymerases (metabolism), Protein Processing, Post-Translational, Proto-Oncogene Proteins (metabolism), RNA (metabolism), Signal Transduction.
- MESH :
- chemical , chemistry : Adenosine Diphosphate, Chromatin, Phosphotransferases (Alcohol Group Acceptor).
- chemical , genetics : ADP Ribose Transferases.
- chemical , metabolism : DNA Repair Enzymes, DNA, Single-Stranded, Hydrolases, NAD, Poly(ADP-ribose) Polymerases, Proto-Oncogene Proteins, RNA.
- metabolism : Escherichia coli, Plasmids.
- ADP-Ribosylation, Adenosine Diphosphate Ribose, Animals, Catalysis, DNA Repair, Humans, Mice, Phosphorylation, Protein Processing, Post-Translational, Signal Transduction.
Abstract
ADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD+) as a cofactor to transfer monomer or polymers of ADP-ribose nucleotide onto macromolecular targets such as proteins and DNA. ADP-ribosylation plays an important role in several biological processes such as DNA repair, transcription, chromatin remodelling, host-virus interactions, cellular stress response and many more. Using biochemical methods we identify RNA as a novel target of reversible mono-ADP-ribosylation. We demonstrate that the human PARPs - PARP10, PARP11 and PARP15 as well as a highly diverged PARP homologue TRPT1, ADP-ribosylate phosphorylated ends of RNA. We further reveal that ADP-ribosylation of RNA mediated by PARP10 and TRPT1 can be efficiently reversed by several cellular ADP-ribosylhydrolases (PARG, TARG1, MACROD1, MACROD2 and ARH3), as well as by MACROD-like hydrolases from VEEV and SARS viruses. Finally, we show that TRPT1 and MACROD homologues in bacteria possess activities equivalent to the human proteins. Our data suggest that RNA ADP-ribosylation may represent a widespread and physiologically relevant form of reversible ADP-ribosylation signalling.
DOI: 10.1093/nar/gkz305
PubMed: 31216043
Affiliations:
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ADP Ribose Transferases (genetics)</term>
<term>ADP-Ribosylation</term>
<term>Adenosine Diphosphate (chemistry)</term>
<term>Adenosine Diphosphate Ribose</term>
<term>Animals</term>
<term>Catalysis</term>
<term>Chromatin (chemistry)</term>
<term>DNA Repair</term>
<term>DNA Repair Enzymes (metabolism)</term>
<term>DNA, Single-Stranded (metabolism)</term>
<term>Escherichia coli (metabolism)</term>
<term>Humans</term>
<term>Hydrolases (metabolism)</term>
<term>Mice</term>
<term>NAD (metabolism)</term>
<term>Phosphorylation</term>
<term>Phosphotransferases (Alcohol Group Acceptor) (chemistry)</term>
<term>Plasmids (metabolism)</term>
<term>Poly(ADP-ribose) Polymerases (metabolism)</term>
<term>Protein Processing, Post-Translational</term>
<term>Proto-Oncogene Proteins (metabolism)</term>
<term>RNA (metabolism)</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ADN simple brin (métabolisme)</term>
<term>ADP ()</term>
<term>ADP ribose transferases (génétique)</term>
<term>ARN (métabolisme)</term>
<term>Adénosine diphosphate ribose</term>
<term>Animaux</term>
<term>Catalyse</term>
<term>Chromatine ()</term>
<term>Enzymes de réparation de l'ADN (métabolisme)</term>
<term>Escherichia coli (métabolisme)</term>
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<term>NAD (métabolisme)</term>
<term>Phosphorylation</term>
<term>Phosphotransferases (Alcohol Group Acceptor) ()</term>
<term>Plasmides (métabolisme)</term>
<term>Poly(ADP-ribose) polymerases (métabolisme)</term>
<term>Protéines proto-oncogènes (métabolisme)</term>
<term>Réparation de l'ADN</term>
<term>Souris</term>
<term>Transduction du signal</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Adenosine Diphosphate</term>
<term>Chromatin</term>
<term>Phosphotransferases (Alcohol Group Acceptor)</term>
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<term>Hydrolases</term>
<term>NAD</term>
<term>Poly(ADP-ribose) Polymerases</term>
<term>Proto-Oncogene Proteins</term>
<term>RNA</term>
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<term>Adenosine Diphosphate Ribose</term>
<term>Animals</term>
<term>Catalysis</term>
<term>DNA Repair</term>
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<term>Mice</term>
<term>Phosphorylation</term>
<term>Protein Processing, Post-Translational</term>
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<term>Maturation post-traductionnelle des protéines</term>
<term>Phosphorylation</term>
<term>Phosphotransferases (Alcohol Group Acceptor)</term>
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<front><div type="abstract" xml:lang="en">ADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD+) as a cofactor to transfer monomer or polymers of ADP-ribose nucleotide onto macromolecular targets such as proteins and DNA. ADP-ribosylation plays an important role in several biological processes such as DNA repair, transcription, chromatin remodelling, host-virus interactions, cellular stress response and many more. Using biochemical methods we identify RNA as a novel target of reversible mono-ADP-ribosylation. We demonstrate that the human PARPs - PARP10, PARP11 and PARP15 as well as a highly diverged PARP homologue TRPT1, ADP-ribosylate phosphorylated ends of RNA. We further reveal that ADP-ribosylation of RNA mediated by PARP10 and TRPT1 can be efficiently reversed by several cellular ADP-ribosylhydrolases (PARG, TARG1, MACROD1, MACROD2 and ARH3), as well as by MACROD-like hydrolases from VEEV and SARS viruses. Finally, we show that TRPT1 and MACROD homologues in bacteria possess activities equivalent to the human proteins. Our data suggest that RNA ADP-ribosylation may represent a widespread and physiologically relevant form of reversible ADP-ribosylation signalling.</div>
</front>
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<Month>12</Month>
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<Month>06</Month>
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<Title>Nucleic acids research</Title>
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<Abstract><AbstractText>ADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD+) as a cofactor to transfer monomer or polymers of ADP-ribose nucleotide onto macromolecular targets such as proteins and DNA. ADP-ribosylation plays an important role in several biological processes such as DNA repair, transcription, chromatin remodelling, host-virus interactions, cellular stress response and many more. Using biochemical methods we identify RNA as a novel target of reversible mono-ADP-ribosylation. We demonstrate that the human PARPs - PARP10, PARP11 and PARP15 as well as a highly diverged PARP homologue TRPT1, ADP-ribosylate phosphorylated ends of RNA. We further reveal that ADP-ribosylation of RNA mediated by PARP10 and TRPT1 can be efficiently reversed by several cellular ADP-ribosylhydrolases (PARG, TARG1, MACROD1, MACROD2 and ARH3), as well as by MACROD-like hydrolases from VEEV and SARS viruses. Finally, we show that TRPT1 and MACROD homologues in bacteria possess activities equivalent to the human proteins. Our data suggest that RNA ADP-ribosylation may represent a widespread and physiologically relevant form of reversible ADP-ribosylation signalling.</AbstractText>
<CopyrightInformation>© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.</CopyrightInformation>
</Abstract>
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