ArticleThe Journal of biological chemistry2012
Functional and structural insights of a Staphylococcus aureus apoptotic-like membrane peptide from a toxin-antitoxin module.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Membrane selectivity and pore formation of SprA1 and SprA2 hemolytic peptides from Staphylococcus aureus type I toxin-antitoxin systems.The FEBS journal · 2025Article
- Insight into the environmental cues modulating the expression of bacterial toxin-antitoxin systems.FEMS microbiology reviews · 2025Review
- Type I toxin-antitoxin systems in bacteria: from regulation to biological functions.EcoSal Plus · 2024Review
- Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023Article
- Article
- Investigation of the Mechanism and Chemistry Underlying Staphylococcus aureusJournal of bacteriology · 2022Article
- RNase III CLASH in MRSA uncovers sRNA regulatory networks coupling metabolism to toxin expression.Nature communications · 2022Article
- Biology and evolution of bacterial toxin-antitoxin systems.Nature reviews. Microbiology · 2022Review
- XRE family transcriptional regulator XtrSs modulates Streptococcus suis fitness under hydrogen peroxide stress.Archives of microbiology · 2022Article
- Bacterial Small Membrane Proteins: the Swiss Army Knife of Regulators at the Lipid Bilayer.Journal of bacteriology · 2022Review
- Review
- Article
- Charged Residues Flanking the Transmembrane Domain of Two Related Toxin-Antitoxin System Toxins Affect Host Response.Toxins · 2021Article
- Toxin-antitoxin systems and their medical applications: current status and future perspective.Applied microbiology and biotechnology · 2021Review
- RNA Regulated Toxin-Antitoxin Systems in Pathogenic Bacteria.Frontiers in cellular and infection microbiology · 2021Review
- Improved growth ofJournal of bacteriology · 2021Article
- A peptide of a type I toxin-antitoxin system inducesProceedings of the National Academy of Sciences of the United States of America · 2020Article
- YSIRK-G/S-directed translocation is required forVirulence · 2020Article
- The Fst/Ldr Family of Type I TA System Toxins: Potential Roles in Stress Response, Metabolism and Pathogenesis.Toxins · 2020Review
- Genome-Wide Screening for Identification of Novel Toxin-Antitoxin Systems in Staphylococcus aureus.Applied and environmental microbiology · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report a functional type I toxin-antitoxin (TA) module expressed by a human pathogen, Staphylococcus aureus. TA systems consist of stable toxins and labile antitoxins encoded within small genetic modules widespread in eubacteria and archaea. TA genes provide stress adaptation and protection against DNA loss or invasion. The genes encoding the SprA1 toxic peptide (PepA1) and the SprA1(AS) RNA antitoxin are within a pathogenicity island on opposite strands and possess a 3' overlap. To prevent peptide toxicity during S. aureus growth, PepA1 expression from stable (half-life > 3 h) SprA1 is repressed by elevated amounts of unstable (half-life = ∼10 mn) SprA1(AS). In vivo, PepA1 localizes at the bacterial membrane and triggers S. aureus death. Based on NMR and CD data, its solution structure was solved and is a long bent, interrupted helix. Molecular dynamics simulations indicate that PepA1 compaction and helical content fluctuate in accordance with its cytoplasm or membrane location. When inserted into the S. aureus membrane, the PepA1 conformation switches to a ∼7-nm-long continuous helix, presumably forming pores to alter membrane integrity. PepA1 expression is induced upon acidic and oxidative stresses by reducing SprA1(AS) levels. As an altruistic behavior during infection, some cells may induce the expression of that toxin that would facilitate departure from the host immune cells for spreading.
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