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ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function

The functionality of DNA, RNA and proteins is altered dynamically in response to physiological and pathological cues, partly achieved by their modification. While the modification of proteins with ADP-ribose has been well studied, nucleic acids were only recently identified as substrates for ADP-rib...

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Autores principales: Weixler, Lisa, Schäringer, Katja, Momoh, Jeffrey, Lüscher, Bernhard, Feijs, Karla L H, Žaja, Roko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8053099/
https://www.ncbi.nlm.nih.gov/pubmed/33693930
http://dx.doi.org/10.1093/nar/gkab136
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author Weixler, Lisa
Schäringer, Katja
Momoh, Jeffrey
Lüscher, Bernhard
Feijs, Karla L H
Žaja, Roko
author_facet Weixler, Lisa
Schäringer, Katja
Momoh, Jeffrey
Lüscher, Bernhard
Feijs, Karla L H
Žaja, Roko
author_sort Weixler, Lisa
collection PubMed
description The functionality of DNA, RNA and proteins is altered dynamically in response to physiological and pathological cues, partly achieved by their modification. While the modification of proteins with ADP-ribose has been well studied, nucleic acids were only recently identified as substrates for ADP-ribosylation by mammalian enzymes. RNA and DNA can be ADP-ribosylated by specific ADP-ribosyltransferases such as PARP1–3, PARP10 and tRNA 2′-phosphotransferase (TRPT1). Evidence suggests that these enzymes display different preferences towards different oligonucleotides. These reactions are reversed by ADP-ribosylhydrolases of the macrodomain and ARH families, such as MACROD1, TARG1, PARG, ARH1 and ARH3. Most findings derive from in vitro experiments using recombinant components, leaving the relevance of this modification in cells unclear. In this Survey and Summary, we provide an overview of the enzymes that ADP-ribosylate nucleic acids, the reversing hydrolases, and the substrates’ requirements. Drawing on data available for other organisms, such as pierisin1 from cabbage butterflies and the bacterial toxin–antitoxin system DarT–DarG, we discuss possible functions for nucleic acid ADP-ribosylation in mammals. Hypothesized roles for nucleic acid ADP-ribosylation include functions in DNA damage repair, in antiviral immunity or as non-conventional RNA cap. Lastly, we assess various methods potentially suitable for future studies of nucleic acid ADP-ribosylation.
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spelling pubmed-80530992021-04-21 ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function Weixler, Lisa Schäringer, Katja Momoh, Jeffrey Lüscher, Bernhard Feijs, Karla L H Žaja, Roko Nucleic Acids Res Survey and Summary The functionality of DNA, RNA and proteins is altered dynamically in response to physiological and pathological cues, partly achieved by their modification. While the modification of proteins with ADP-ribose has been well studied, nucleic acids were only recently identified as substrates for ADP-ribosylation by mammalian enzymes. RNA and DNA can be ADP-ribosylated by specific ADP-ribosyltransferases such as PARP1–3, PARP10 and tRNA 2′-phosphotransferase (TRPT1). Evidence suggests that these enzymes display different preferences towards different oligonucleotides. These reactions are reversed by ADP-ribosylhydrolases of the macrodomain and ARH families, such as MACROD1, TARG1, PARG, ARH1 and ARH3. Most findings derive from in vitro experiments using recombinant components, leaving the relevance of this modification in cells unclear. In this Survey and Summary, we provide an overview of the enzymes that ADP-ribosylate nucleic acids, the reversing hydrolases, and the substrates’ requirements. Drawing on data available for other organisms, such as pierisin1 from cabbage butterflies and the bacterial toxin–antitoxin system DarT–DarG, we discuss possible functions for nucleic acid ADP-ribosylation in mammals. Hypothesized roles for nucleic acid ADP-ribosylation include functions in DNA damage repair, in antiviral immunity or as non-conventional RNA cap. Lastly, we assess various methods potentially suitable for future studies of nucleic acid ADP-ribosylation. Oxford University Press 2021-03-08 /pmc/articles/PMC8053099/ /pubmed/33693930 http://dx.doi.org/10.1093/nar/gkab136 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Survey and Summary
Weixler, Lisa
Schäringer, Katja
Momoh, Jeffrey
Lüscher, Bernhard
Feijs, Karla L H
Žaja, Roko
ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function
title ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function
title_full ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function
title_fullStr ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function
title_full_unstemmed ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function
title_short ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function
title_sort adp-ribosylation of rna and dna: from in vitro characterization to in vivo function
topic Survey and Summary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8053099/
https://www.ncbi.nlm.nih.gov/pubmed/33693930
http://dx.doi.org/10.1093/nar/gkab136
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