ArticleThe Journal of biological chemistry2016
The Type IV Pilus Assembly ATPase PilB of Myxococcus xanthus Interacts with the Inner Membrane Platform Protein PilC and the Nucleotide-binding Protein PilM.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 75 citations in OpenAlex.
- Discovery of PilU as a second type IV pilus retraction motor inJournal of bacteriology · 2026Article
- A broad-spectrum phage-encoded mechanism to disarm bacterial type IV filaments.PLoS pathogens · 2026Article
- A broad-spectrum phage-encoded mechanism to disarm bacterial type IV filaments.bioRxiv : the preprint server for biology · 2026Article
- Electron Cryo-Tomography Reveals thebioRxiv : the preprint server for biology · 2025Article
- Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025Article
- Milestones in the development ofJournal of bacteriology · 2025Review
- The role of PilU in the surface behaviors ofmLife · 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
- Type IV pili ofEcoSal Plus · 2024Review
- Combinatorial control of type IVa pili formation by the four polarized regulators MglA, SgmX, FrzS, and SopA.Journal of bacteriology · 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
- Membrane platform protein PulF of themBio · 2024Article
- A cyanobacterial chemotaxis-like system controls phototactic orientation via phosphorylation of two antagonistic response regulators.microLife · 2024Article
- Mechanism of assembly of type 4 filaments: everything you always wanted to know (but were afraid to ask).Microbiology (Reading, England) · 2023Review
- Characterising ATP binding activity of PilB ATPase ofJournal of biosciences · 2023Article
- Adaptations to high pressure of Nautilia sp. strain PV-1, a piezophilic Campylobacterium (aka Epsilonproteobacterium) isolated from a deep-sea hydrothermal vent.Environmental microbiology · 2022Article
- Landmark Discoveries and Recent Advances in Type IV Pilus Research.Microbiology and molecular biology reviews : MMBR · 2022Review
- Retraction ATPase Motors from Three Orthologous Type IVa Pilus Systems Support Promiscuous Retraction of the Vibrio cholerae Competence Pilus.Journal of bacteriology · 2022Article
- Towards Elucidating the Rotary Mechanism of the Archaellum Machinery.Frontiers in microbiology · 2022Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type IV pili (T4P) are ubiquitous bacterial cell surface structures, involved in processes such as twitching motility, biofilm formation, bacteriophage infection, surface attachment, virulence, and natural transformation. T4P are assembled by machinery that can be divided into the outer membrane pore complex, the alignment complex that connects components in the inner and outer membrane, and the motor complex in the inner membrane and cytoplasm. Here, we characterize the inner membrane platform protein PilC, the cytosolic assembly ATPase PilB of the motor complex, and the cytosolic nucleotide-binding protein PilM of the alignment complex of the T4P machinery ofMyxococcus xanthus PilC was purified as a dimer and reconstituted into liposomes. PilB was isolated as a monomer and bound ATP in a non-cooperative manner, but PilB fused to Hcp1 ofPseudomonas aeruginosaformed a hexamer and bound ATP in a cooperative manner. Hexameric but not monomeric PilB bound to PilC reconstituted in liposomes, and this binding stimulated PilB ATPase activity. PilM could only be purified when it was stabilized by a fusion with a peptide corresponding to the first 16 amino acids of PilN, supporting an interaction between PilM and PilN(1-16). PilM-N(1-16) was isolated as a monomer that bound but did not hydrolyze ATP. PilM interacted directly with PilB, but only with PilC in the presence of PilB, suggesting an indirect interaction. We propose that PilB interacts with PilC and with PilM, thus establishing the connection between the alignment and the motor complex.
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