ArticleProceedings of the National Academy of Sciences of the United States of America2019
ParST is a widespread toxin-antitoxin module that targets nucleotide metabolism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- A survey of ADP-ribosyltransferase families in the pathogenic Legionella.BMC genomics · 2025Article
- A bacterial toxin-antitoxin system involved in an unusual response to genotoxic stress.EMBO reports · 2025Article
- Structural basis for higher-order DNA binding by a bacterial transcriptional regulator.PLoS genetics · 2025Article
- RES-Xre toxin-antitoxin locusEmerging microbes & infections · 2024Article
- Toxin-mediated depletion of NAD and NADP drives persister formation in a human pathogen.The EMBO journal · 2024Article
- Search for Origins of Anti-CRISPR Proteins by Structure Comparison.The CRISPR journal · 2023Article
- The DarT/DarG Toxin-Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies.Pathogens (Basel, Switzerland) · 2023Article
- Biology and evolution of bacterial toxin-antitoxin systems.Nature reviews. Microbiology · 2022Review
- Article
- Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases.Toxins · 2021Review
- ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021Review
- Genome Mining Shows Ubiquitous Presence and Extensive Diversity of Toxin-Antitoxin Systems inFrontiers in microbiology · 2021Article
- Bacterial type II toxin-antitoxin systems acting through post-translational modifications.Computational and structural biotechnology journal · 2021Review
- Article
- Review
- Review
- Novel Toxin-Antitoxin Module SlvT-SlvA Regulates Megaplasmid Stability and Incites Solvent Tolerance in Pseudomonas putida S12.Applied and environmental microbiology · 2020Article
- Targeting ADP-ribosylation as an antimicrobial strategy.Biochemical pharmacology · 2019Review
- Characterization of Two Toxin-Antitoxin Systems in Deep-SeaMarine drugs · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Toxin-antitoxin (TA) systems interfere with essential cellular processes and are implicated in bacterial lifestyle adaptations such as persistence and the biofilm formation. Here, we present structural, biochemical, and functional data on an uncharacterized TA system, the COG5654-COG5642 pair. Bioinformatic analysis showed that this TA pair is found in 2,942 of the 16,286 distinct bacterial species in the RefSeq database. We solved a structure of the toxin bound to a fragment of the antitoxin to 1.50 Å. This structure suggested that the toxin is a mono-ADP-ribosyltransferase (mART). The toxin specifically modifies phosphoribosyl pyrophosphate synthetase (Prs), an essential enzyme in nucleotide biosynthesis conserved in all organisms. We propose renaming the toxin ParT for Prs ADP-ribosylating toxin and ParS for the cognate antitoxin. ParT is a unique example of an intracellular protein mART in bacteria and is the smallest known mART. This work demonstrates that TA systems can induce bacteriostasis through interference with nucleotide biosynthesis.
Indexed as
Identifiers
What OpenQuestion holds
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.