ArticleNature communications2014
Multiple enzymatic activities of ParB/Srx superfamily mediate sexual conflict among conjugative plasmids.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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.
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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.
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Who cites it
23 citing papers in PubMed, 32 citations in OpenAlex.
- Conjugative transfer inhibition of IncA and IncC plasmids by SGI1-like elements via relaxosome assembly interference.Nucleic acids research · 2026Article
- Plasmid-encoded host reprogramming promotes plasmid dissemination.bioRxiv : the preprint server for biology · 2026Article
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- Expanding the landscape of BREX diversity: uncovering multi-layered functional frameworks and identification of novel BREX-related defense systems.Nucleic acids research · 2026Article
- The extended mobility of plasmids.Nucleic acids research · 2025Review
- Unveiling the multifaceted domain polymorphism of the Menshen antiphage system.Nucleic acids research · 2025Article
- TIGR-Tas: A family of modular RNA-guided DNA-targeting systems in prokaryotes and their viruses.Science (New York, N.Y.) · 2025Article
- Two novel phages infectingFrontiers in microbiology · 2025Article
- Molecular basis of the phosphorothioation-sensing antiphage defense system IscS-DndBCDE-DndI.Nucleic acids research · 2024Article
- Reappraisal of the DNA phosphorothioate modification machinery: uncovering neglected functional modalities and identification of new counter-invader defense systems.Nucleic acids research · 2024Article
- Functionally comparable but evolutionarily distinct nucleotide-targeting effectors help identify conserved paradigms across diverse immune systems.Nucleic acids research · 2023Article
- New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts.NAR genomics and bioinformatics · 2023Article
- Towards a better understanding of antimicrobial resistance dissemination: what can be learnt from studying model conjugative plasmids?Military Medical Research · 2022Review
- Comprehensive classification of ABC ATPases and their functional radiation in nucleoprotein dynamics and biological conflict systems.Nucleic acids research · 2020Review
- SspABCD-SspE is a phosphorothioation-sensing bacterial defence system with broad anti-phage activities.Nature microbiology · 2020Article
- Article
- SbnI is a free serine kinase that generatesThe Journal of biological chemistry · 2018Article
- Natural and Artificial Strategies To Control the Conjugative Transmission of Plasmids.Microbiology spectrum · 2018Review
- Polyvalent Proteins, a Pervasive Theme in the Intergenomic Biological Conflicts of Bacteriophages and Conjugative Elements.Journal of bacteriology · 2017Article
- PifC and Osa, Plasmid Weapons against Rival Conjugative Coupling Proteins.Frontiers in microbiology · 2017Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Conjugative plasmids are typically locked in intergenomic and sexual conflicts with co-resident rivals, whose translocation they block using fertility inhibition factors (FINs). We describe here the first crystal structure of an enigmatic FIN Osa deployed by the proteobacterial plasmid pSa. Osa contains a catalytically active version of the ParB/Sulfiredoxin fold with both ATPase and DNase activity, the latter being regulated by an ATP-dependent switch. Using the Agrobacterium tumefaciens VirB/D4 type IV secretion system (T4SS), a relative of the conjugative T4SS, we demonstrate that catalytically active Osa blocks T-DNA transfer into plants. With a partially reconstituted T4SS in vitro, we show that Osa degrades T-DNA in the T-DNA-VirD2 complex before its translocation. Further, we present evidence for conservation and interplay between ATPase and DNase activities throughout the ParB/Sulfiredoxin fold, using other members of the family, namely P1 ParB and RK2 KorB, which have general functional implications across diverse biological contexts.
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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.