ArticleThe Journal of biological chemistry2015
Pseudomonas aeruginosa minor pilins prime type IVa pilus assembly and promote surface display of the PilY1 adhesin.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.
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Who cites it
100 citing papers in PubMed.
- β-strand addition within tip initiation complexes licenses assembly of diverse type IV filaments.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Insight into the relationship between type IV pilus function and biofilm formation.Biochemical Society transactions · 2026Review
- The stoichiometry of minor-to-major pilins regulates the dynamic activity of the type IVa competence pilus in Vibrio cholerae.PLoS genetics · 2026Article
- Visualization of Type IV Pili: Linking Structural Architecture, Dynamic Function, and Translational Opportunities.Biology · 2026Review
- PilY proteins: bimodular drivers of type IV pilus versatility.Trends in microbiology · 2026Review
- Defining the role ofJournal of bacteriology · 2026Article
- Phage cocktails containing a dual-receptorApplied and environmental microbiology · 2026Article
- β-strand complementation within tip initiation complexes licenses assembly of diverse type IV filaments.bioRxiv : the preprint server for biology · 2026Article
- A prophage-expressed type IV pilus component provides anti-phage defense.Cell reports · 2026Article
- Diversity, classification, and evolution of myxobacterial PilY1 proteins.Frontiers in microbiology · 2026Article
- Proteomic Analysis of the Differential Response ofAntibiotics (Basel, Switzerland) · 2025Article
- Separation ofmBio · 2025Article
- Article
- Improved DNA binding to a type IV minor pilin increases natural transformation.Nucleic acids research · 2025Article
- Article
- Tad pili with adaptable tips mediate contact-dependent killing during bacterial predation.Nature communications · 2025Article
- The molecular basis for DNA-binding by competence T4P is distinct in a representative Gram-positive and Gram-negative species.PLoS pathogens · 2025Article
- Review
- Structural conservation and functional role of TfpY-like proteins in type IV pilus assembly.Journal of bacteriology · 2025Article
- Host-mimicking conditions promoteFrontiers in microbiology · 2025Article
40 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
Abstract
Type IV pili (T4P) contain hundreds of major subunits, but minor subunits are also required for assembly and function. Here we show that Pseudomonas aeruginosa minor pilins prime pilus assembly and traffic the pilus-associated adhesin and anti-retraction protein, PilY1, to the cell surface. PilV, PilW, and PilX require PilY1 for inclusion in surface pili and vice versa, suggestive of complex formation. PilE requires PilVWXY1 for inclusion, suggesting that it binds a novel interface created by two or more components. FimU is incorporated independently of the others and is proposed to couple the putative minor pilin-PilY1 complex to the major subunit. The production of small amounts of T4P by a mutant lacking the minor pilin operon was traced to expression of minor pseudopilins from the P. aeruginosa type II secretion (T2S) system, showing that under retraction-deficient conditions, T2S minor subunits can prime T4P assembly. Deletion of all minor subunits abrogated pilus assembly. In a strain lacking the minor pseudopilins, PilVWXY1 and either FimU or PilE comprised the minimal set of components required for pilus assembly. Supporting functional conservation of T2S and T4P minor components, our 1.4 Å crystal structure of FimU revealed striking architectural similarity to its T2S ortholog GspH, despite minimal sequence identity. We propose that PilVWXY1 form a priming complex for assembly and that PilE and FimU together stably couple the complex to the major subunit. Trafficking of the anti-retraction factor PilY1 to the cell surface allows for production of pili of sufficient length to support adherence and motility.
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