Reversible ADP-ribosylation of RNA
<p>ADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD<sup>+</sup>) as a cofactor to transfer monomer or polymers of ADP-ribose nucleotide onto macromolecular targets such as p...
| 主要な著者: | , , , , , , , |
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| フォーマット: | Journal article |
| 出版事項: |
Oxford University Press
2019
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| _version_ | 1826285216448118784 |
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| author | Munnur, D Bartlett, E Mikolcevic, P Kirby, I Rack, J Mikoc, A Cohen, M Ahel, I |
| author_facet | Munnur, D Bartlett, E Mikolcevic, P Kirby, I Rack, J Mikoc, A Cohen, M Ahel, I |
| author_sort | Munnur, D |
| collection | OXFORD |
| description | <p>ADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD<sup>+</sup>) 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.</p> |
| first_indexed | 2024-03-07T01:25:31Z |
| format | Journal article |
| id | oxford-uuid:91daf908-2c7c-4d46-856f-d687b96a58a1 |
| institution | University of Oxford |
| last_indexed | 2024-03-07T01:25:31Z |
| publishDate | 2019 |
| publisher | Oxford University Press |
| record_format | dspace |
| spelling | oxford-uuid:91daf908-2c7c-4d46-856f-d687b96a58a12022-03-26T23:21:26ZReversible ADP-ribosylation of RNAJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:91daf908-2c7c-4d46-856f-d687b96a58a1Symplectic Elements at OxfordOxford University Press2019Munnur, DBartlett, EMikolcevic, PKirby, IRack, JMikoc, ACohen, MAhel, I<p>ADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD<sup>+</sup>) 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.</p> |
| spellingShingle | Munnur, D Bartlett, E Mikolcevic, P Kirby, I Rack, J Mikoc, A Cohen, M Ahel, I Reversible ADP-ribosylation of RNA |
| title | Reversible ADP-ribosylation of RNA |
| title_full | Reversible ADP-ribosylation of RNA |
| title_fullStr | Reversible ADP-ribosylation of RNA |
| title_full_unstemmed | Reversible ADP-ribosylation of RNA |
| title_short | Reversible ADP-ribosylation of RNA |
| title_sort | reversible adp ribosylation of rna |
| work_keys_str_mv | AT munnurd reversibleadpribosylationofrna AT bartlette reversibleadpribosylationofrna AT mikolcevicp reversibleadpribosylationofrna AT kirbyi reversibleadpribosylationofrna AT rackj reversibleadpribosylationofrna AT mikoca reversibleadpribosylationofrna AT cohenm reversibleadpribosylationofrna AT aheli reversibleadpribosylationofrna |