SrasV1, Main, Exploration, bibRecord, 000A99

Reversible ADP-ribosylation of RNA.

Identifieur interne : 000A99 ( Main/Exploration ); précédent : 000A98; suivant : 000B00

Reversible 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.

RBID : pubmed:31216043

Descripteurs français

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:

Le document en format XML

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<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>
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<term>Proto-Oncogene Proteins (metabolism)</term>
<term>RNA (metabolism)</term>
<term>Signal Transduction</term>
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<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>
<term>Humains</term>
<term>Hydrolases (métabolisme)</term>
<term>Maturation post-traductionnelle des protéines</term>
<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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<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>Plasmides</term>
<term>Poly(ADP-ribose) polymerases</term>
<term>Protéines proto-oncogènes</term>
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<term>Catalysis</term>
<term>DNA Repair</term>
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<term>Mice</term>
<term>Phosphorylation</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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Reversible ADP-ribosylation of RNA.

Reversible ADP-ribosylation of RNA.

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