ArticleScientific reports2018
ClpAP protease is a universal factor that activates the parDE toxin-antitoxin system from a broad host range RK2 plasmid.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 14 citations in OpenAlex.
- Transcriptomic insights on differential gene regulations in viable but non-culturable (VBNC) bacteria under chlorine and UV disinfection.BMC microbiology · 2026Article
- Single-cell evidence for plasmid addiction mediated by toxin-antitoxin systems.Nucleic acids research · 2024Article
- Bacterial Toxin-Antitoxin Systems' Cross-Interactions-Implications for Practical Use in Medicine and Biotechnology.Toxins · 2023Review
- A ParDE toxin-antitoxin system is responsible for the maintenance of theFrontiers in cellular and infection microbiology · 2023Article
- Bacterial toxin-antitoxin systems: Novel insights on toxin activation across populations and experimental shortcomings.Current research in microbial sciences · 2023Review
- Biology and evolution of bacterial toxin-antitoxin systems.Nature reviews. Microbiology · 2022Review
- Article
- Cellular functions of the ClpP protease impacting bacterial virulence.Frontiers in molecular biosciences · 2022Review
- Cellular Self-Digestion and Persistence in Bacteria.Microorganisms · 2021Review
- Control of Toxin-Antitoxin Systems by Proteases inFrontiers in molecular biosciences · 2021Review
- DNA and Polyphosphate in Directed Proteolysis for DNA Replication Control.Frontiers in microbiology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activity of type II toxin-antitoxin systems (TA), which are responsible for many important features of bacterial cells, is based on the differences between toxin and antitoxin stabilities. The antitoxin lability results from bacterial protease activity. Here, we investigated how particular Escherichia coli cytosolic proteases, namely, Lon, ClpAP, ClpXP, and ClpYQ, affect the stability of both the toxin and antitoxin components of the parDE system from the broad host range plasmid RK2. The results of our in vivo and in vitro experiments show that the ParD antitoxin is degraded by the ClpAP protease, and dsDNA stimulates this process. The ParE toxin is not degraded by any of these proteases and can therefore cause growth inhibition of plasmid-free cells after an unequal plasmid distribution during cell division. We also demonstrate that the ParE toxin interaction with ParD prevents antitoxin proteolysis by ClpAP; however, this interaction does not prevent the ClpAP interaction with ParD. We show that ClpAP protease homologs affect plasmid stability in other bacterial species, indicating that ClpAP is a universal activator of the parDE system and that ParD is a universal substrate for ClpAP.
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.