Reversible ADP-ribosylation of RNA.
Identifieur interne : 000896 ( PubMed/Corpus ); précédent : 000895; suivant : 000897Reversible ADP-ribosylation of RNA.
Auteurs : Deeksha Munnur ; Edward Bartlett ; Petra Mikol Evi ; Ilsa T. Kirby ; Johannes Gregor Matthias Rack ; Andreja Miko ; Michael S. Cohen ; Ivan AhelSource :
- Nucleic acids research [ 1362-4962 ] ; 2019.
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
Links to Exploration step
pubmed:31216043Le document en format XML
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Kirby</name><affiliation><nlm:affiliation>Program in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health and Science University, Portland, OR 97239, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Matthias Rack, Johannes Gregor" sort="Matthias Rack, Johannes Gregor" uniqKey="Matthias Rack J" first="Johannes Gregor" last="Matthias Rack">Johannes Gregor Matthias Rack</name><affiliation><nlm:affiliation>Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Miko, Andreja" sort="Miko, Andreja" uniqKey="Miko A" first="Andreja" last="Miko">Andreja Miko</name><affiliation><nlm:affiliation>Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.</nlm:affiliation></affiliation></author><author><name sortKey="Cohen, Michael S" sort="Cohen, Michael S" uniqKey="Cohen M" first="Michael S" last="Cohen">Michael S. Cohen</name><affiliation><nlm:affiliation>Program in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health and Science University, Portland, OR 97239, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Ahel, Ivan" sort="Ahel, Ivan" uniqKey="Ahel I" first="Ivan" last="Ahel">Ivan Ahel</name><affiliation><nlm:affiliation>Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Nucleic acids research</title><idno type="eISSN">1362-4962</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><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="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Adenosine Diphosphate</term><term>Chromatin</term><term>Phosphotransferases (Alcohol Group Acceptor)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>ADP Ribose Transferases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA Repair Enzymes</term><term>DNA, Single-Stranded</term><term>Hydrolases</term><term>NAD</term><term>Poly(ADP-ribose) Polymerases</term><term>Proto-Oncogene Proteins</term><term>RNA</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Plasmids</term></keywords><keywords scheme="MESH" xml:lang="en"><term>ADP-Ribosylation</term><term>Adenosine Diphosphate Ribose</term><term>Animals</term><term>Catalysis</term><term>DNA Repair</term><term>Humans</term><term>Mice</term><term>Phosphorylation</term><term>Protein Processing, Post-Translational</term><term>Signal Transduction</term></keywords></textClass></profileDesc></teiHeader><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></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31216043</PMID><DateCompleted><Year>2019</Year><Month>12</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1362-4962</ISSN><JournalIssue CitedMedium="Internet"><Volume>47</Volume><Issue>11</Issue><PubDate><Year>2019</Year><Month>06</Month><Day>20</Day></PubDate></JournalIssue><Title>Nucleic acids research</Title><ISOAbbreviation>Nucleic Acids Res.</ISOAbbreviation></Journal><ArticleTitle>Reversible ADP-ribosylation of RNA.</ArticleTitle><Pagination><MedlinePgn>5658-5669</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/nar/gkz305</ELocationID><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><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Munnur</LastName><ForeName>Deeksha</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bartlett</LastName><ForeName>Edward</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mikolčević</LastName><ForeName>Petra</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kirby</LastName><ForeName>Ilsa T</ForeName><Initials>IT</Initials><AffiliationInfo><Affiliation>Program in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health and Science University, Portland, OR 97239, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matthias Rack</LastName><ForeName>Johannes Gregor</ForeName><Initials>JG</Initials><AffiliationInfo><Affiliation>Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mikoč</LastName><ForeName>Andreja</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cohen</LastName><ForeName>Michael S</ForeName><Initials>MS</Initials><AffiliationInfo><Affiliation>Program in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health and Science University, Portland, OR 97239, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ahel</LastName><ForeName>Ivan</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><Acronym>WT_</Acronym><Agency>Wellcome Trust</Agency><Country>United Kingdom</Country></Grant><Grant><Acronym>BB_</Acronym><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>R01 NS088629</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nucleic Acids Res</MedlineTA><NlmUniqueID>0411011</NlmUniqueID><ISSNLinking>0305-1048</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002843">Chromatin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004277">DNA, Single-Stranded</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C523332">MACROD2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011518">Proto-Oncogene Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0U46U6E8UK</RegistryNumber><NameOfSubstance UI="D009243">NAD</NameOfSubstance></Chemical><Chemical><RegistryNumber>20762-30-5</RegistryNumber><NameOfSubstance UI="D000246">Adenosine Diphosphate Ribose</NameOfSubstance></Chemical><Chemical><RegistryNumber>61D2G4IYVH</RegistryNumber><NameOfSubstance UI="D000244">Adenosine Diphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.2.-</RegistryNumber><NameOfSubstance UI="D036002">ADP Ribose Transferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.2.30</RegistryNumber><NameOfSubstance UI="C499627">PARP10 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.2.30</RegistryNumber><NameOfSubstance UI="D011065">Poly(ADP-ribose) Polymerases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="C527101">Trpt1 protein, mouse</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.-</RegistryNumber><NameOfSubstance UI="D006867">Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.5.1.-</RegistryNumber><NameOfSubstance UI="D045643">DNA Repair Enzymes</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D036002" MajorTopicYN="N">ADP Ribose Transferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000074744" MajorTopicYN="Y">ADP-Ribosylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000244" MajorTopicYN="N">Adenosine Diphosphate</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000246" MajorTopicYN="N">Adenosine Diphosphate Ribose</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011065" MajorTopicYN="N">Poly(ADP-ribose) Polymerases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011518" MajorTopicYN="N">Proto-Oncogene Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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