ArticleThe Journal of biological chemistry2009
The XcpV/GspI pseudopilin has a central role in the assembly of a quaternary complex within the T2SS pseudopilus.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed.
- Surface Plasmon Resonance: A Sensitive Tool to Study Protein-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Ab Initio Modelling of the Structure of ToxA-like and MAX Fungal Effector Proteins.International journal of molecular sciences · 2023Article
- Characterization of a glycan-binding complex of minor pilins completes the analysis ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Prophage-encoded gene VpaChn25_0734 amplifies ecological persistence of Vibrio parahaemolyticus CHN25.Current genetics · 2022Article
- The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation.Nature communications · 2022Article
- The Role of Minor Pilins in Assembly and Function of the Competence Pilus ofFrontiers in cellular and infection microbiology · 2021Article
- GspD, The Type II Secretion System Secretin ofVaccines · 2020Article
- PilY1 and minor pilins form a complex priming the type IVa pilus in Myxococcus xanthus.Nature communications · 2020Article
- In Situ Proteolysis Condition-Induced Crystallization of the XcpVWX Complex in Different Lattices.International journal of molecular sciences · 2020Article
- In vivo structure of the Legionella type II secretion system by electron cryotomography.Nature microbiology · 2019Article
- Assessing the impact, genomics and evolution of type II secretion across a large, medically important genus: the Legionella type II secretion paradigm.Microbial genomics · 2019Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Direct interactions between the secreted effector and the T2SS components GspL and GspM reveal a new effector-sensing step during type 2 secretion.The Journal of biological chemistry · 2018Article
- Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa.PLoS pathogens · 2018Article
- The Vibrio cholerae Minor Pilin TcpB Initiates Assembly and Retraction of the Toxin-Coregulated Pilus.PLoS pathogens · 2016Article
- Pseudomonas aeruginosa minor pilins prime type IVa pilus assembly and promote surface display of the PilY1 adhesin.The Journal of biological chemistry · 2015Article
- Editorial.FEMS microbiology reviews · 2015Article
- Exceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knives.FEMS microbiology reviews · 2015Review
- Complex formation and processing of the minor transformation pilins of Bacillus subtilis.Molecular microbiology · 2013Article
- Dynamic interplay between the periplasmic and transmembrane domains of GspL and GspM in the type II secretion system.PloS one · 2013Article
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8 authors.
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Abstract
Gram-negative bacteria use the sophisticated type II secretion system (T2SS) to secrete a large number of exoproteins into the extracellular environment. Five proteins of the T2SS, the pseudopilins GspG-H-I-J-K, are proposed to assemble into a pseudopilus involved in the extrusion of the substrate through the outer membrane channel. Recent structural data have suggested that the three pseudopilins GspI-J-K are organized in a trimeric complex located at the tip of the GspG-containing pseudopilus. In the present work we combined two biochemical techniques to investigate the protein-protein interaction network between the five Pseudomonas aeruginosa Xcp pseudopilins. The soluble domains of XcpT-U-V-W-X (respectively homologous to GspG-H-I-J-K) were purified, and the interactions were tested by surface plasmon resonance and affinity co-purification in all possible combinations. We found an XcpV(I)-W(J)-X(K) complex, which demonstrates that the crystallized trimeric complex also exists in the P. aeruginosa T2SS. Interestingly, our systematic approach revealed an additional and yet uncharacterized interaction between XcpU(H) and XcpW(J). This observation suggested the existence of a quaternary, rather than ternary, complex (XcpU(H)-V(I)-W(J)-X(K)) at the tip of the pseudopilus. The assembly of this quaternary complex was further demonstrated by co-purification using affinity chromatography. Moreover, by testing various combinations of pseudopilins by surface plasmon resonance and affinity chromatography, we were able to dissect the different possible successive steps occurring during the formation of the quaternary complex. We propose a model in which XcpV(I) is the nucleator that first binds XcpX(K) and XcpW(J) at different sites. Then the ternary complex recruits XcpU(H) through a direct interaction with XcpW(J).
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