ArticleThe Biochemical journal2002
XpsG, the major pseudopilin in Xanthomonas campestris pv. campestris, forms a pilus-like structure between cytoplasmic and outer membranes.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 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
- Secrete or perish: The role of secretion systems inComputational and structural biotechnology journal · 2021Review
- GspD, The Type II Secretion System Secretin ofVaccines · 2020Article
- 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
- 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
- The type II secretion system: biogenesis, molecular architecture and mechanism.Nature reviews. Microbiology · 2012Review
- Deciphering the Xcp Pseudomonas aeruginosa type II secretion machinery through multiple interactions with substrates.The Journal of biological chemistry · 2011Article
- The assembly mode of the pseudopilus: a hallmark to distinguish a novel secretion system subtype.The Journal of biological chemistry · 2011Article
- Involvement of the GspAB complex in assembly of the type II secretion system secretin of Aeromonas and Vibrio species.Journal of bacteriology · 2011Article
- In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae.Molecular microbiology · 2011Article
- The XcpV/GspI pseudopilin has a central role in the assembly of a quaternary complex within the T2SS pseudopilus.The Journal of biological chemistry · 2009Article
- PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus.Journal of bacteriology · 2008Article
- Structure of the minor pseudopilin EpsH from the Type 2 secretion system of Vibrio cholerae.Journal of molecular biology · 2008Article
- The crystal structure of a binary complex of two pseudopilins: EpsI and EpsJ from the type 2 secretion system of Vibrio vulnificus.Journal of molecular biology · 2008Article
- The TadV protein of Actinobacillus actinomycetemcomitans is a novel aspartic acid prepilin peptidase required for maturation of the Flp1 pilin and TadE and TadF pseudopilins.Journal of bacteriology · 2006Article
- XpsE oligomerization triggered by ATP binding, not hydrolysis, leads to its association with XpsL.The EMBO journal · 2006Article
- The ins and outs of DNA transfer in bacteria.Science (New York, N.Y.) · 2005Review
- Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca.Journal of bacteriology · 2005Article
- Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure.Journal of bacteriology · 2003Article
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7 authors.
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Abstract
GspG, -H, -I, -J and -K proteins are members of the pseudopilin family. They are the components required for the type II secretion pathway, which translocates proteins across the outer membrane of Gram-negative bacteria to the extracellular milieu. They were predicted to form a pilus-like structure, and this has been shown for PulG of Klebsiella oxytoca by using electron microscopy. In the present study, we performed biochemical analyses of the XpsG protein of Xanthomonas campestris pv. campestris and observed that it is a pillar-like structure spanning the cytoplasmic and outer membranes. Subcellular fractionation revealed a soluble form (SF) of XpsG, in addition to the membrane form. Chromatographic analysis of SF XpsG in the absence of a detergent indicated that it is part of a large complex (>440 kDa). In vitro studies indicated that XpsG is prone to aggregate in the absence of a detergent. We isolated and characterized a non-functional mutant defective in forming the large complex. It did not interfere with the function of wild-type XpsG and was not detectable in the SF. Moreover, unlike wild-type XpsG, which was distributed in both the cytoplasmic and outer membranes, it appeared only in the cytoplasmic membrane. When wild-type XpsG was co-expressed with His6-tagged XpsH but not with untagged XpsH, SF XpsG bound to nickel and co-eluted with XpsH. This result suggests the presence of other pseudopilin components in the XpsG-containing large-sized molecules.
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