ArticleThe Journal of biological chemistry2010
Vibrio cholerae ParE2 poisons DNA gyrase via a mechanism distinct from other gyrase inhibitors.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 73 citations in OpenAlex.
- Broken beyond repair: TA system ParE toxins mediate effective gyrase inhibition without driving resistance.Journal of bacteriology · 2025Article
- Toxin release by conditional remodelling of ParDE1 from Mycobacterium tuberculosis leads to gyrase inhibition.Nucleic acids research · 2024Article
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Toxin:antitoxin ratio sensing autoregulation of theScience advances · 2024Article
- Type II bacterial toxin-antitoxins: hypotheses, facts, and the newfound plethora of the PezAT system.FEMS microbiology reviews · 2023Article
- Article
- Applications of toxin-antitoxin systems in synthetic biology.Engineering microbiology · 2023Review
- Not Quite Lost in Translation: Mistranslation Alters Adaptive Landscape Topography and the Dynamics of Evolution.Molecular biology and evolution · 2023Article
- A ParDE toxin-antitoxin system is responsible for the maintenance of theFrontiers in cellular and infection microbiology · 2023Article
- Toxin-antitoxin systems in pathogenic3 Biotech · 2022Review
- Article
- Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin.Acta crystallographica. Section D, Structural biology · 2021Article
- Toxin-antitoxin systems and their medical applications: current status and future perspective.Applied microbiology and biotechnology · 2021Review
- Uncovering the basis of protein-protein interaction specificity with a combinatorially complete library.eLife · 2020Article
- Review
- The Variety in the Common Theme of Translation Inhibition by Type II Toxin-Antitoxin Systems.Frontiers in genetics · 2020Review
- Expression of different ParE toxins results in conserved phenotypes with distinguishable classes of toxicity.MicrobiologyOpen · 2019Article
- TASmania: A bacterial Toxin-Antitoxin Systems database.PLoS computational biology · 2019Article
- Article
- The toxin from a ParDE toxin-antitoxin system found in Pseudomonas aeruginosa offers protection to cells challenged with anti-gyrase antibiotics.Molecular microbiology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
DNA gyrase is an essential bacterial enzyme required for the maintenance of chromosomal DNA topology. This enzyme is the target of several protein toxins encoded in toxin-antitoxin (TA) loci as well as of man-made antibiotics such as quinolones. The genome of Vibrio cholerae, the cause of cholera, contains three putative TA loci that exhibit modest similarity to the RK2 plasmid-borne parDE TA locus, which is thought to target gyrase although its mechanism of action is uncharacterized. Here we investigated the V. cholerae parDE2 locus. We found that this locus encodes a functional proteic TA pair that is active in Escherichia coli as well as V. cholerae. ParD2 co-purified with ParE2 and interacted with it directly. Unlike many other antitoxins, ParD2 could prevent but not reverse ParE2 toxicity. ParE2, like the unrelated F-encoded toxin CcdB and quinolones, targeted the GyrA subunit and stalled the DNA-gyrase cleavage complex. However, in contrast to other gyrase poisons, ParE2 toxicity required ATP, and it interfered with gyrase-dependent DNA supercoiling but not DNA relaxation. ParE2 did not bind GyrA fragments bound by CcdB and quinolones, and a set of strains resistant to a variety of known gyrase inhibitors all exhibited sensitivity to ParE2. Together, our findings suggest that ParE2 and presumably its many plasmid- and chromosome-encoded homologues inhibit gyrase in a different manner than previously described agents.
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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.