ArticleThe Journal of biological chemistry2011
The assembly mode of the pseudopilus: a hallmark to distinguish a novel secretion system subtype.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structures of the Xcp and Hxc T2SS endopili provide new insights into type IV pili subfamilies.Structure (London, England : 1993) · 2026Article
- Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa.PLoS pathogens · 2018Article
- Article
- Txc, a new type II secretion system of Pseudomonas aeruginosa strain PA7, is regulated by the TtsS/TtsR two-component system and directs specific secretion of the CbpE chitin-binding protein.Journal of bacteriology · 2014Article
- Distinct docking and stabilization steps of the Pseudopilus conformational transition path suggest rotational assembly of type IV pilus-like fibers.Structure (London, England : 1993) · 2014Article
- The rise of the Type VI secretion system.F1000prime reports · 2013Review
- Proteinaceous determinants of surface colonization in bacteria: bacterial adhesion and biofilm formation from a protein secretion perspective.Frontiers in microbiology · 2013Review
- Type IV pilin proteins: versatile molecular modules.Microbiology and molecular biology reviews : MMBR · 2012Review
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Protein Secretion Systems in Pseudomonas aeruginosa: An Essay on Diversity, Evolution, and Function.Frontiers in microbiology · 2011Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In gram-negative bacteria, type II secretion systems assemble a piston-like structure, called pseudopilus, which expels exoproteins out of the cell. The pseudopilus is constituted by a major pseudopilin that when overproduced multimerizes into a long cell surface structure named hyper-pseudopilus. Pseudomonas aeruginosa possesses two type II secretion systems, Xcp and Hxc. Although major pseudopilins are exchangeable among type II secretion systems, we show that XcpT and HxcT are not. We demonstrate that HxcT does not form a hyper-pseudopilus and is different in amino acid sequence and multimerization properties. Using structure-based mutagenesis, we observe that five mutations are sufficient to revert HxcT into a functional XcpT-like protein, which also becomes capable of forming a hyper-pseudopilus. Phylogenetic and experimental analysis showed that the whole Hxc system was acquired by P. aeruginosa PAO1 and other Pseudomonas species through horizontal gene transfer. We thus identified a new type II secretion subfamily, of which the P. aeruginosa Hxc system is the archetype. This finding demonstrates how similar bacterial machineries evolve toward distinct mechanisms that may contribute specific functions.
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