ADP-ribosylation of DNA and RNA.
ADP-ribosylation
DNA damage response
DNA modification
PARP
RNA modification
Journal
DNA repair
ISSN: 1568-7856
Titre abrégé: DNA Repair (Amst)
Pays: Netherlands
ID NLM: 101139138
Informations de publication
Date de publication:
09 2021
09 2021
Historique:
received:
18
03
2021
revised:
28
05
2021
accepted:
31
05
2021
pubmed:
12
6
2021
medline:
13
10
2021
entrez:
11
6
2021
Statut:
ppublish
Résumé
ADP-ribosylation is a chemical modification of macromolecules found across all domains of life and known to regulate a variety of cellular processes. Notably, it has a well-established role in the DNA damage response. While it was historically known as a post-translational modification of proteins, recent studies have shown that nucleic acids can also serve as substrates of reversible ADP-ribosylation. More precisely, ADP-ribosylation of DNA bases, phosphorylated DNA ends and phosphorylated RNA ends have been reported. We will discuss these three types of modification in details. In a variety of bacterial species, including Mycobacterium tuberculosis, ADP-ribosylation of thymidine has emerged as the mode of action of a toxin-antitoxin system named DarTG, with the resultant products perceived as DNA damage by the cell. On the other hand, mammalian DNA damage sensors PARP1, PARP2 and PARP3 were shown to ADP-ribosylate phosphorylated ends of double-stranded DNA in vitro. Additionally, TRPT1 and several PARP enzymes, including PARP10, can add ADP-ribose to the 5'-phosphorylated end of single-stranded RNA in vitro, representing a novel RNA capping mechanism. Together, these discoveries have led to the emergence of a new and exciting research area, namely DNA and RNA ADP-ribosylation, that is likely to have far-reaching implications for the fields of DNA repair, replication and epigenetics.
Identifiants
pubmed: 34116477
pii: S1568-7864(21)00100-2
doi: 10.1016/j.dnarep.2021.103144
pmc: PMC8385414
pii:
doi:
Substances chimiques
Cell Cycle Proteins
0
Proto-Oncogene Proteins
0
RNA
63231-63-0
DNA
9007-49-2
PARP1 protein, human
EC 2.4.2.30
PARP10 protein, human
EC 2.4.2.30
PARP2 protein, human
EC 2.4.2.30
PARP3 protein, human
EC 2.4.2.30
Poly (ADP-Ribose) Polymerase-1
EC 2.4.2.30
Poly(ADP-ribose) Polymerases
EC 2.4.2.30
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
103144Subventions
Organisme : Wellcome Trust
ID : 210634
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R007195/1
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C35050/A22284
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 210634
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 101794
Pays : United Kingdom
Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier B.V. All rights reserved.
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