ArticleThe Journal of biological chemistry2016
PilN Binding Modulates the Structure and Binding Partners of the Pseudomonas aeruginosa Type IVa Pilus 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 40 papers.
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Who cites it
40 citing papers in PubMed, 61 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
- Separation ofmBio · 2025Article
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- Phage reprogramming ofmBio · 2025Article
- Building permits-control of type IV pilus assembly by PilB and its cofactors.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
- PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa.Nature communications · 2024Article
- A bacterial sense of touch: T4P retraction motor as a means of surface sensing byJournal of bacteriology · 2024Review
- Probable Role of Type IV Pili ofPathogens (Basel, Switzerland) · 2024Article
- Bacterial flagella hijack type IV pili proteins to control motility.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Inhibition of PQS signaling by the Pf bacteriophage protein PfsE enhances viral replication in Pseudomonas aeruginosa.Molecular microbiology · 2024Article
- Structure of a heteropolymeric type 4 pilus from a monoderm bacterium.Nature communications · 2023Article
- Evidence for the Type IV Pilus Retraction Motor PilT as a Component of the Surface Sensing System in Pseudomonas aeruginosa.Journal of bacteriology · 2023Article
- Functional annotation of uncharacterized proteins from Fusobacterium nucleatum: identification of virulence factors.Genomics & informatics · 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
- Review
- Landmark Discoveries and Recent Advances in Type IV Pilus Research.Microbiology and molecular biology reviews : MMBR · 2022Review
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Pseudomonas aeruginosa is an opportunistic bacterial pathogen that expresses type IVa pili. The pilus assembly system, which promotes surface-associated twitching motility and virulence, is composed of inner and outer membrane subcomplexes, connected by an alignment subcomplex composed of PilMNOP. PilM binds to the N terminus of PilN, and we hypothesize that this interaction causes functionally significant structural changes in PilM. To characterize this interaction, we determined the crystal structures of PilM and a PilM chimera where PilM was fused to the first 12 residues of PilN (PilM·PilN(1-12)). Structural analysis, multiangle light scattering coupled with size exclusion chromatography, and bacterial two-hybrid data revealed that PilM forms dimers mediated by the binding of a novel conserved motif in the N terminus of PilM, and binding PilN abrogates this binding interface, resulting in PilM monomerization. Structural comparison of PilM with PilM·PilN(1-12) revealed that upon PilN binding, there is a large domain closure in PilM that alters its ATP binding site. Using biolayer interferometry, we found that the association rate of PilN with PilM is higher in the presence of ATP compared with ADP. Bacterial two-hybrid data suggested the connectivity of the cytoplasmic and inner membrane components of the type IVa pilus machinery in P. aeruginosa, with PilM binding to PilB, PilT, and PilC in addition to PilN. Pull-down experiments demonstrated direct interactions of PilM with PilB and PilT. We propose a working model in which dynamic binding of PilN facilitates functionally relevant structural changes in PilM.
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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.