ArticleJournal of bacteriology2002
Identification of XcpZ domains required for assembly of the secreton of Pseudomonas aeruginosa.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa.Scientific reports · 2018Article
- Type IV Pilus Alignment Subcomplex Proteins PilN and PilO Form Homo- and Heterodimers in Vivo.The Journal of biological chemistry · 2016Article
- Dynamic interplay between the periplasmic and transmembrane domains of GspL and GspM in the type II secretion system.PloS one · 2013Article
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Docking and assembly of the type II secretion complex of Vibrio cholerae.Journal of bacteriology · 2009Article
- Mapping critical interactive sites within the periplasmic domain of the Vibrio cholerae type II secretion protein EpsM.Journal of bacteriology · 2007Article
- Functional dissection of the XpsN (GspC) protein of the Xanthomonas campestris pv. campestris type II secretion machinery.Journal of bacteriology · 2004Article
- A reversibly dissociable ternary complex formed by XpsL, XpsM and XpsN of the Xanthomonas campestris pv. campestris type II secretion apparatus.The Biochemical journal · 2002Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most of the exoproteins secreted by Pseudomonas aeruginosa are transported via the type II secretion system. This machinery, which is widely conserved in gram-negative bacteria, consists of 12 Xcp proteins organized as a multiprotein complex, also called the secreton. We previously reported that the mutual stabilization of XcpZ and XcpY plays an important role in the assembly of the secreton. In this study, we engineered variant XcpZ proteins by using linker insertion mutagenesis. We identified three distinct regions of XcpZ required for both the stabilization of XcpY and the functionality of the secreton. Interestingly, we also demonstrated that another component of the machinery, XcpP, can modulate the stabilizing activity of XcpZ on XcpY.
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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.