Pathogens · 2023 · 12 citations · 118 references
Life SciencesBiochemistryMolecular BiologyEnzymologyPost-translational ModificationStructural BiologyEnzyme FunctionRna StructureChemical ModificationEvolutionary Conservation Of DomainsMycobacterium Tuberculosis InfectionMycobacterium Tuberculosis PathogenesisRational DesignRibonucleotide ChemistryStress Response MechanismsToxin-antitoxin Systems
The chemical modification of cellular macromolecules by the transfer of ADP-ribose unit(s), known as ADP-ribosylation, is an ancient homeostatic and stress response control system. Highly conserved across the evolution, ADP-ribosyltransferases and ADP-ribosylhydrolases control ADP-ribosylation signalling and cellular responses. In addition to proteins, both prokaryotic and eukaryotic transferases can covalently link ADP-ribosylation to different conformations of nucleic acids, thus highlighting the evolutionary conservation of archaic stress response mechanisms. Here, we report several structural and functional aspects of DNA ADP-ribosylation modification controlled by the prototype DarT and DarG pair, which show ADP-ribosyltransferase and hydrolase activity, respectively. DarT/DarG is a toxin–antitoxin system conserved in many bacterial pathogens, for example in Mycobacterium tuberculosis, which regulates two clinically important processes for human health, namely, growth control and the anti-phage response. The chemical modulation of the DarT/DarG system by selective inhibitors may thus represent an exciting strategy to tackle resistance to current antimicrobial therapies.
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Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
Damien D’Amours, Serge Desnoyers, Icy D’Silva et al. · Biochemical Journal · 1999 · 1.8K citations · Full text
Systematic and quantitative view of the antiviral arsenal of prokaryotes
Florian Tesson, Hervé Alexandre, Ernest Mordret et al. · Nature Communications · 2022 · 765 citations · Full text
Poly(ADP-ribose)–Dependent Regulation of DNA Repair by the Chromatin Remodeling Enzyme ALC1
Dragana Ahel, Zuzana Hořejšı́, Nicola Wiechens et al. · Science · 2009 · 596 citations · Full text