ArticlePLoS pathogens2017
Convergent evolution involving dimeric and trimeric dUTPases in pathogenicity island mobilization.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- dUTPase modulates mycobacterial homologous recombination and interacts with the AdnAB helicase-nuclease.Nucleic acids research · 2026Article
- Analysis of SalHV-1 Genes by Structure Prediction and Comparison Shows an Expanded Core Gene Set of the OrderViruses · 2026Article
- Is dUTPase Enzymatic Activity Truly Essential for Viability?International journal of molecular sciences · 2025Review
- Genetics, ecology and evolution of phage satellites.Nature reviews. Microbiology · 2025Review
- Metaviromic analyses of DNA virus community from sediments of the N-Choe stream, North India.Virus research · 2023Article
- The Bacteriophage-Phage-Inducible Chromosomal Island Arms Race Designs an Interkingdom Inhibitor of dUTPases.Microbiology spectrum · 2023Article
- Insights into the mechanism of action of the arbitrium communication system in SPbeta phages.Nature communications · 2022Article
- Viral dUTPases: Modulators of Innate Immunity.Biomolecules · 2022Review
- Phage satellites and their emerging applications in biotechnology.FEMS microbiology reviews · 2021Review
- Article
- The structure of a polygamous repressor reveals how phage-inducible chromosomal islands spread in nature.Nature communications · 2019Article
- Article
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Authors and funding
9 authors.
Funding
Abstract
The dUTPase (Dut) enzymes, encoded by almost all free-living organisms and some viruses, prevent the misincorporation of uracil into DNA. We previously proposed that trimeric Duts are regulatory proteins involved in different cellular processes; including the phage-mediated transfer of the Staphylococcus aureus pathogenicity island SaPIbov1. Recently, it has been shown that the structurally unrelated dimeric Dut encoded by phage ϕNM1 is similarly able to mobilize SaPIbov1, suggesting dimeric Duts could also be regulatory proteins. How this is accomplished remains unsolved. Here, using in vivo, biochemical and structural approaches, we provide insights into the signaling mechanism used by the dimeric Duts to induce the SaPIbov1 cycle. As reported for the trimeric Duts, dimeric Duts contain an extremely variable region, here named domain VI, which is involved in the regulatory capacity of these enzymes. Remarkably, our results also show that the dimeric Dut signaling mechanism is modulated by dUTP, as with the trimeric Duts. Overall, our results demonstrate that although unrelated both in sequence and structure, dimeric and trimeric Duts control SaPI transfer by analogous mechanisms, representing a fascinating example of convergent evolution. This conserved mode of action highlights the biological significance of Duts as regulatory molecules.
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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.