ArticleNucleic acids research2022
Non-canonical Staphylococcus aureus pathogenicity island repression.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Phage induction of Staphylococcus aureus pathogenicity islands promotes the CRISPR-Cas adaptive immune response.Cell reports · 2026Article
- Genetics, ecology and evolution of phage satellites.Nature reviews. Microbiology · 2025Review
- Phage parasites targeting phage homologous recombinases provide antiviral immunity.Nature communications · 2025Article
- Tail assembly interference is a common strategy in bacterial antiviral defenses.Nature communications · 2024Article
- Nucleoid-associated proteins shape the global protein occupancy and transcriptional landscape of a clinical isolate ofmSphere · 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
- Induction mechanisms and strategies underlying interprophage competition during polylysogeny.PLoS pathogens · 2023Article
- Horizontal transfer of probable chicken-pathogenicity chromosomal islands between Staphylococcus aureus and Staphylococcus agnetis.PloS one · 2023Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Mobile genetic elements control their life cycles by the expression of a master repressor, whose function must be disabled to allow the spread of these elements in nature. Here, we describe an unprecedented repression-derepression mechanism involved in the transfer of Staphylococcus aureus pathogenicity islands (SaPIs). Contrary to the classical phage and SaPI repressors, which are dimers, the SaPI1 repressor StlSaPI1 presents a unique tetrameric conformation never seen before. Importantly, not just one but two tetramers are required for SaPI1 repression, which increases the novelty of the system. To derepress SaPI1, the phage-encoded protein Sri binds to and induces a conformational change in the DNA binding domains of StlSaPI1, preventing the binding of the repressor to its cognate StlSaPI1 sites. Finally, our findings demonstrate that this system is not exclusive to SaPI1 but widespread in nature. Overall, our results characterize a novel repression-induction system involved in the transfer of MGE-encoded virulence factors in nature.
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