ArticleNature communications2019
The structure of a polygamous repressor reveals how phage-inducible chromosomal islands spread in nature.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Genetics, ecology and evolution of phage satellites.Nature reviews. Microbiology · 2025Review
- Phage parasites targeting phage homologous recombinases provide antiviral immunity.Nature communications · 2025Article
- Full-length inhibitor protein is the most effective to perturb human dUTPase activity.Scientific reports · 2025Article
- The homodimerization domain of the Stl repressor is crucial for efficient inhibition of mycobacterial dUTPase.Scientific reports · 2024Article
- Antirepressor specificity is shaped by highly efficient dimerization of the staphylococcal pathogenicity island regulating repressors: Stl repressor dimerization perturbed by dUTPases.Scientific reports · 2024Article
- The Bacteriophage-Phage-Inducible Chromosomal Island Arms Race Designs an Interkingdom Inhibitor of dUTPases.Microbiology spectrum · 2023Article
- Non-canonical Staphylococcus aureus pathogenicity island repression.Nucleic acids research · 2022Article
- Insights into the mechanism of action of the arbitrium communication system in SPbeta phages.Nature communications · 2022Article
- Redox status of cysteines does not alter functional properties of human dUTPase but the Y54C mutation involved in monogenic diabetes decreases protein stability.Scientific reports · 2021Article
- Phylogeny Reveals Novel HipA-Homologous Kinase Families and Toxin-Antitoxin Gene Organizations.mBio · 2021Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Stl is a master repressor encoded by Staphylococcus aureus pathogenicity islands (SaPIs) that maintains integration of these elements in the bacterial chromosome. After infection or induction of a resident helper phage, SaPIs are de-repressed by specific interactions of phage proteins with Stl. SaPIs have evolved a fascinating mechanism to ensure their promiscuous transfer by targeting structurally unrelated proteins performing identically conserved functions for the phage. Here we decipher the molecular mechanism of this elegant strategy by determining the structure of SaPIbov1 Stl alone and in complex with two structurally unrelated dUTPases from different S. aureus phages. Remarkably, SaPIbov1 Stl has evolved different domains implicated in DNA and partner recognition specificity. This work presents the solved structure of a SaPI repressor protein and the discovery of a modular repressor that acquires multispecificity through domain recruiting. Our results establish the mechanism that allows widespread dissemination of SaPIs in nature.
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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.