Diamond Publications - Search Results

Search Again...

These results include publications that have not yet been reviewed and processed by Diamond Light Source. To view only processed publications click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

One item found (0 items not approved).

Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	Molecular basis for the reversible ADP-ribosylation of guanosine bases Marion Schuller , Roberto Raggiaschi , Petra Mikolcevic , Johannes G. M. Rack , Antonio Ariza , Yugeng Zhang , Raphael Ledermann , Christoph Tang , Andreja Mikoc , Ivan Ahel Molecular Cell 116 DOI: 10.1016/j.molcel.2023.06.013 Diamond Proposal Number(s): [23459] Open Access Show Abstract ▼ Abstract: 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.	Jun 2023

Instruments / Technical Area

Publication Details

Published

Actions

I03-Macromolecular Crystallography

Molecular basis for the reversible ADP-ribosylation of guanosine bases

Marion Schuller , Roberto Raggiaschi , Petra Mikolcevic , Johannes G. M. Rack , Antonio Ariza , Yugeng Zhang , Raphael Ledermann , Christoph Tang , Andreja Mikoc , Ivan Ahel

Molecular Cell 116

DOI: 10.1016/j.molcel.2023.06.013

Diamond Proposal Number(s): [23459]