ArticleJournal of bacteriology2008
PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
98 citing papers in PubMed, 156 citations in OpenAlex.
- Discovery of PilU as a second type IV pilus retraction motor inJournal of bacteriology · 2026Article
- Tandem receiver domain response regulator DrdR modulates swarming by controlling PilB/PilT activity inmLife · 2026Article
- A broad-spectrum phage-encoded mechanism to disarm bacterial type IV filaments.PLoS pathogens · 2026Article
- Article
- PilY proteins: bimodular drivers of type IV pilus versatility.Trends in microbiology · 2026Review
- Article
- Twitching motility suppressors reveal a role for FimX in type IV pilus extension dynamics.PLoS genetics · 2025Article
- Milestones in the development ofJournal of bacteriology · 2025Review
- Xanthomonas oryzae Orphan Response Regulator EmvR Is Involved in Virulence, Extracellular Polysaccharide Production and Cell Motility.Molecular plant pathology · 2025Article
- Unusual cell surfaces, pili, and archaella of Thermoplasmatales archaea.The ISME journal · 2025Article
- Saccharibacteria deploy two distinct type IV pili, driving episymbiosis, host competition, and twitching motility.The ISME journal · 2025Article
- Building permits-control of type IV pilus assembly by PilB and its cofactors.Journal of bacteriology · 2024Review
- Architectural dissection of adhesive bacterial cell surface appendages from a "molecular machines" viewpoint.Journal of bacteriology · 2024Review
- Saccharibacteria deploy two distinct Type IV pili, driving episymbiosis, host competition, and twitching motility.bioRxiv : the preprint server for biology · 2024Article
- Combinatorial control of type IVa pili formation by the four polarized regulators MglA, SgmX, FrzS, and SopA.Journal of bacteriology · 2024Article
- Coaggregation Occurs between a Piliated Unicellular Cyanobacterium,Microorganisms · 2024Article
- A deterministic, c-di-GMP-dependent program ensures the generation of phenotypically similar, symmetric daughter cells during cytokinesis.Nature communications · 2024Article
- A cyanobacterial chemotaxis-like system controls phototactic orientation via phosphorylation of two antagonistic response regulators.microLife · 2024Article
- Article
- Molecular basis and design principles of switchable front-rear polarity and directional migration in Myxococcus xanthus.Nature communications · 2023Article
38 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type IV pili (T4P) are dynamic surface structures that undergo cycles of extension and retraction. T4P dynamics center on the PilB and PilT proteins, which are members of the secretion ATPase superfamily of proteins. Here, we show that PilB and PilT of the T4P system in Myxococcus xanthus have ATPase activity in vitro. Using a structure-guided approach, we systematically mutagenized PilB and PilT to resolve whether both ATP binding and hydrolysis are important for PilB and PilT function in vivo. PilB as well as PilT ATPase activity was abolished in vitro by replacement of conserved residues in the Walker A and Walker B boxes that are involved in ATP binding and hydrolysis, respectively. PilB proteins containing mutant Walker A or Walker B boxes were nonfunctional in vivo and unable to support T4P extension. PilT proteins containing mutant Walker A or Walker B boxes were also nonfunctional in vivo and unable to support T4P retraction. These data provide genetic evidence that both ATP binding and hydrolysis by PilB are essential for T4P extension and that both ATP binding and hydrolysis by PilT are essential for T4P retraction. Thus, PilB and PilT are ATPases that act at distinct steps in the T4P extension/retraction cycle in vivo.
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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.