ArticleMolecular cell2015
Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens.
Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 98 citations in OpenAlex.
- The BRCT domain enhances DNA binding and catalytic efficiency of fungal PARPs.Nature communications · 2026Article
- Integrated multi-omics reveals coordinatedmSystems · 2026Article
- Molecular basis for anti-jumbo phage immunity by AVAST type 5.Molecular cell · 2026Article
- Unraveling proteomic chaos by independent component analysis-ClpX proficiency promotes the iron and oxygen limitation responses ofmSystems · 2025Article
- Filament formation and NAD processing by noncanonical human FAM118 sirtuins.Nature structural & molecular biology · 2025Article
- Staphylococcus aureus exploits lipoic acid salvage to combat host oxidative stress.Cell reports · 2025Article
- In Silico Characterization of Sirtuins in Acetic Acid Bacteria Reveals a Novel Phylogenetically Distinctive Group.Molecules (Basel, Switzerland) · 2025Article
- Dynamics of diversified A-to-I editing in Streptococcus pyogenes is governed by changes in mRNA stability.Nucleic acids research · 2024Article
- Sirtuin E deacetylase is required for full virulence of Aspergillus fumigatus.Communications biology · 2024Article
- Exploring the targetome of IsrR, an iron-regulated sRNA controlling the synthesis of iron-containing proteins inFrontiers in microbiology · 2024Article
- The dual role of sirtuins in cancer: biological functions and implications.Frontiers in oncology · 2024Review
- Article
- Functionally comparable but evolutionarily distinct nucleotide-targeting effectors help identify conserved paradigms across diverse immune systems.Nucleic acids research · 2023Article
- Review
- The DarT/DarG Toxin-Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies.Pathogens (Basel, Switzerland) · 2023Article
- Design, synthesis, and pharmacological evaluations of pyrrolo[1,2-a]quinoxaline-based derivatives as potent and selective sirt6 activators.European journal of medicinal chemistry · 2023Article
- Apprehending the NADViruses · 2022Article
- Intracellular mono-ADP-ribosyltransferases at the host-virus interphase.Cellular and molecular life sciences : CMLS · 2022Review
- Beyond protein modification: the rise of non-canonical ADP-ribosylation.The Biochemical journal · 2022Article
- Deletion of rifampicin-inactivating mono-ADP-ribosyl transferase gene ofCurrent research in microbial sciences · 2022Article
Corrections and comments
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Authors and funding
14 authors at 6 institutions in 3 countries.
Funding
Abstract
Sirtuins are an ancient family of NAD(+)-dependent deacylases connected with the regulation of fundamental cellular processes including metabolic homeostasis and genome integrity. We show the existence of a hitherto unrecognized class of sirtuins, found predominantly in microbial pathogens. In contrast to earlier described classes, these sirtuins exhibit robust protein ADP-ribosylation activity. In our model organisms, Staphylococcus aureus and Streptococcus pyogenes, the activity is dependent on prior lipoylation of the target protein and can be reversed by a sirtuin-associated macrodomain protein. Together, our data describe a sirtuin-dependent reversible protein ADP-ribosylation system and establish a crosstalk between lipoylation and mono-ADP-ribosylation. We propose that these posttranslational modifications modulate microbial virulence by regulating the response to host-derived reactive oxygen species.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.