ArticleNature communications2020
Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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Who cites it
38 citing papers in PubMed, 66 citations in OpenAlex.
- Insight into the relationship between type IV pilus function and biofilm formation.Biochemical Society transactions · 2026Review
- Major type IV pilin ofmBio · 2026Article
- Visualization of Type IV Pili: Linking Structural Architecture, Dynamic Function, and Translational Opportunities.Biology · 2026Review
- Ultrastructural and atomic characterization of biofilm-associated extracellular filaments in Shewanella oneidensis MR-1.Nature communications · 2026Article
- Structural insights into the Thermus thermophilus type IV pilus machinery assembling two distinct pili.Communications biology · 2026Article
- Segmented filamentous bacteria undergo a structural transition at their adhesive tip during unicellular to filament development.Nature communications · 2025Article
- Structural insights into the secretin complex of a type IVb pilus system.Nature communications · 2025Article
- Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025Article
- Coming Clean and Avoiding Bubble Trouble-Using Detergents Wisely in the Purification of Membrane Proteins for Cryo-EM Studies.Biomolecules · 2025Review
- Form and function in biological filaments: a physicist's review.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025Review
- Review
- Saccharibacteria deploy two distinct type IV pili, driving episymbiosis, host competition, and twitching motility.The ISME journal · 2025Article
- Biochemical characterization of theFrontiers in microbiology · 2025Article
- The 1.3 Å resolution structure of the truncated group Ia type IV pilin from Pseudomonas aeruginosa strain P1.Acta crystallographica. Section D, Structural biology · 2024Article
- Structure of the Pseudomonas aeruginosa PAO1 Type IV pilus.PLoS pathogens · 2024Article
- Saccharibacteria deploy two distinct Type IV pili, driving episymbiosis, host competition, and twitching motility.bioRxiv : the preprint server for biology · 2024Article
- Structural diversity and clustering of bacterial flagellar outer domains.Nature communications · 2024Article
- Structural mechanisms of Tad pilus assembly and its interaction with an RNA virus.Science advances · 2024Article
- Tight-packing of large pilin subunits provides distinct structural and mechanical properties for theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus ('wide' and 'narrow'), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility.
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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.