ArticleJournal of bacteriology2001
Exchange of Xcp (Gsp) secretion machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes: species specificity unrelated to substrate recognition.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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
12 citing papers in PubMed, 32 citations in OpenAlex.
- Insights into dynamics and gating properties of T2SS secretins.Science advances · 2023Article
- Filamentous phages: masters of a microbial sharing economy.EMBO reports · 2019Review
- Unraveling the Self-Assembly of themBio · 2017Article
- Expanding Role of Type II Secretion in Bacterial Pathogenesis and Beyond.Infection and immunity · 2017Review
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The assembly mode of the pseudopilus: a hallmark to distinguish a novel secretion system subtype.The Journal of biological chemistry · 2011Article
- Glucose depletion in the airway surface liquid is essential for sterility of the airways.PloS one · 2011Article
- Protein Secretion Systems in Pseudomonas aeruginosa: An Essay on Diversity, Evolution, and Function.Frontiers in microbiology · 2011Article
- Phosphate starvation triggers production and secretion of an extracellular lipoprotein in Caulobacter crescentus.PloS one · 2010Article
- HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor.The Journal of biological chemistry · 2009Article
- XphA/XqhA, a novel GspCD subunit for type II secretion in Pseudomonas aeruginosa.Journal of bacteriology · 2007Article
- Species-specific functioning of the Pseudomonas XcpQ secretin: role for the C-terminal homology domain and lipopolysaccharide.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas aeruginosa and Pseudomonas alcaligenes are gram-negative bacteria that secrete proteins using the type II or general secretory pathway, which requires at least 12 xcp gene products (XcpA and XcpP to -Z). Despite strong conservation of this secretion pathway, gram-negative bacteria usually cannot secrete exoproteins from other species. Based on results obtained with Erwinia, it has been proposed that the XcpP and/or XcpQ homologs determine this secretion specificity (M. Linderberg, G. P. Salmond, and A. Collmer, Mol. Microbiol. 20:175-190, 1996). In the present study, we report that XcpP and XcpQ of P. alcaligenes could not substitute for their respective P. aeruginosa counterparts. However, these complementation failures could not be correlated to species-specific recognition of exoproteins, since these bacteria could secrete exoproteins of each other. Moreover, when P. alcaligenes xcpP and xcpQ were expressed simultaneously in a P. aeruginosa xcpPQ deletion mutant, complementation was observed, albeit only on agar plates and not in liquid cultures. After growth in liquid culture the heat-stable P. alcaligenes XcpQ multimers were not detected, whereas monomers were clearly visible. Together, our results indicate that the assembly of a functional Xcp machinery requires species-specific interactions between XcpP and XcpQ and between XcpP or XcpQ and another, as yet uncharacterized component(s).
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