Molecular basis for the reversible ADP-ribosylation of guanosine bases.

Guanosine ADP-Ribosylation ADP Ribose Transferases / genetics Eukaryotic Cells / metabolism Antitoxins / genetics Adenosine Diphosphate Ribose / metabolism
ADP-ribosylation ADP-ribosyltransferases DNA damage DNA modifications PARP toxin-antitoxin system

Journal

Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571

Informations de publication

Date de publication:
06 07 2023
Historique:
received: 10 11 2022
revised: 13 04 2023
accepted: 08 06 2023
medline: 10 7 2023
pubmed: 1 7 2023
entrez: 30 6 2023
Statut: ppublish

Résumé

Modification of nucleic acids by ADP-ribosylation is catalyzed by various ADP-ribosyltransferases, including the DarT enzyme. The latter is part of the bacterial toxin-antitoxin (TA) system DarTG, which was shown to provide control of DNA replication and bacterial growth as well as protection against bacteriophages. Two subfamilies have been identified, DarTG1 and DarTG2, which are distinguished by their associated antitoxins. While DarTG2 catalyzes reversible ADP-ribosylation of thymidine bases employing a macrodomain as antitoxin, the DNA ADP-ribosylation activity of DarTG1 and the biochemical function of its antitoxin, a NADAR domain, are as yet unknown. Using structural and biochemical approaches, we show that DarT1-NADAR is a TA system for reversible ADP-ribosylation of guanosine bases. DarT1 evolved the ability to link ADP-ribose to the guanine amino group, which is specifically hydrolyzed by NADAR. We show that guanine de-ADP-ribosylation is also conserved among eukaryotic and non-DarT-associated NADAR members, indicating a wide distribution of reversible guanine modifications beyond DarTG systems.

Identifiants

DOI: 10.1016/j.molcel.2023.06.013 PMID: 37390817
pubmed: 37390817
pii: S1097-2765(23)00457-4
doi: 10.1016/j.molcel.2023.06.013
pii:
doi:

Substances chimiques

Guanosine 12133JR80S
ADP Ribose Transferases EC 2.4.2.-
Antitoxins 0
Adenosine Diphosphate Ribose 20762-30-5

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2303-2315.e6

Subventions

Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R007195/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/W016613/1
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 210634
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 223107
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C35050/A22284
Pays : United Kingdom

Informations de copyright

Copyright © 2023 The Author(s). Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

Auteurs

Marion Schuller (M)

Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.

Roberto Raggiaschi (R)

Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.

Petra Mikolcevic (P)

Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.

Johannes G M Rack (JGM)

Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.

Antonio Ariza (A)

School of Biosciences, University of Sheffield, Sheffield, UK.

YuGeng Zhang (Y)

Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.

Raphael Ledermann (R)

Department of Biology, University of Oxford, Oxford, UK.

Christoph Tang (C)

Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.

Andreja Mikoc (A)

Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.

Ivan Ahel (I)

Sir William Dunn School of Pathology, University of Oxford, Oxford, UK. Electronic address: ivan.ahel@path.ox.ac.uk.

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Classifications MeSH

questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Nucléosides › Ribonucléosides › Guanosine › Molecular basis for the reversible...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › ADP-Ribosylation › Molecular basis for the reversible...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Glycosyltransferase › Pentosyltransferases › ADP ribose transferases › Molecular basis for the reversible...
questionsmedicales.fr › Cellules › Cellules eucaryotes › Molecular basis for the reversible...
questionsmedicales.fr › Mélanges complexes › Produits biologiques › Sérums immuns › Antitoxines › Molecular basis for the reversible...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Nucléotides › Ribonucléotides › Nucléoside diphosphate ose › Adénosine diphosphate ose › Adénosine diphosphate ribose › Molecular basis for the reversible...