ArticlePLoS genetics2019
The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase.
Article in PLoS genetics, 2019. 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, 52 citations in OpenAlex.
- Discovery of PilU as a second type IV pilus retraction motor inJournal of bacteriology · 2026Article
- Structural modeling reveals the mechanism of motor ATPase coordination during type IV pilus retraction.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Analysis of the heterogenous structural states of the hexameric ATPase PilU of the type IV pili from Vibrio cholerae.Protein science : a publication of the Protein Society · 2026Article
- Analysis of the heterogenous structural states of the hexameric ATPase PilU of the Type IV pili frombioRxiv : the preprint server for biology · 2026Article
- The type IV pilus steering committee: how Pil-Chp controls directional motility.Journal of bacteriology · 2025Review
- Separation ofmBio · 2025Article
- Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025Article
- A global perspective on the genomics ofMicrobial genomics · 2025Article
- Beyond movement: the dynamic roles of Type IV pili in cyanobacterial life.Journal of bacteriology · 2025Review
- Environmental DNA adsorption to chitin can promote horizontal gene transfer by natural transformation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The role of PilU in the surface behaviors ofmLife · 2025Article
- Naturally competent bacteria and their genetic parasites-a battle for control over horizontal gene transfer?FEMS microbiology reviews · 2025Review
- A Phage-Based Approach to Identify Antivirulence Inhibitors of Bacterial Type IV Pili.Microbial biotechnology · 2025Article
- Architectural dissection of adhesive bacterial cell surface appendages from a "molecular machines" viewpoint.Journal of bacteriology · 2024Review
- Building permits-control of type IV pilus assembly by PilB and its cofactors.Journal of bacteriology · 2024Review
- A bacterial sense of touch: T4P retraction motor as a means of surface sensing byJournal of bacteriology · 2024Review
- Type IV pilus retraction is required formBio · 2024Article
- Evidence for the Type IV Pilus Retraction Motor PilT as a Component of the Surface Sensing System in Pseudomonas aeruginosa.Journal of bacteriology · 2023Article
- Evidence for the Type IV Pili Retraction Motor PilT as a Component of the Surface Sensing System inbioRxiv : the preprint server for biology · 2023Article
- The PilT retraction ATPase promotes both extension and retraction of the MSHA type IVa pilus in Vibrio cholerae.PLoS genetics · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Type IV pili are dynamic cell surface appendages found throughout the bacteria. The ability of these structures to undergo repetitive cycles of extension and retraction underpins their crucial roles in adhesion, motility and natural competence for transformation. In the best-studied systems a dedicated retraction ATPase PilT powers pilus retraction. Curiously, a second presumed retraction ATPase PilU is often encoded immediately downstream of pilT. However, despite the presence of two potential retraction ATPases, pilT deletions lead to a total loss of pilus function, raising the question of why PilU fails to take over. Here, using the DNA-uptake pilus and mannose-sensitive haemagglutinin (MSHA) pilus of Vibrio cholerae as model systems, we show that inactivated PilT variants, defective for either ATP-binding or hydrolysis, have unexpected intermediate phenotypes that are PilU-dependent. In addition to demonstrating that PilU can function as a bona fide retraction ATPase, we go on to make the surprising discovery that PilU functions exclusively in a PilT-dependent manner and identify a naturally occurring pandemic V. cholerae PilT variant that renders PilU essential for pilus function. Finally, we show that Pseudomonas aeruginosa PilU also functions as a PilT-dependent retraction ATPase, providing evidence that the functional coupling between PilT and PilU could be a widespread mechanism for optimal pilus retraction.
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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.