ArticleJournal of bacteriology2005
Mapping of a YscY binding domain within the LcrH chaperone that is required for regulation of Yersinia type III secretion.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- Dynamic interaction of the Yersinia pseudotuberculosis type three secretion system proteins LcrV and LcrG.Protein science : a publication of the Protein Society · 2026Article
- Article
- The type III secretion chaperone SctY may shield the hydrophobic export gate-binding C-terminus of its substrate SctX.Acta crystallographica. Section D, Structural biology · 2023Article
- Direct interaction of a chaperone-bound type III secretion substrate with the export gate.Nature communications · 2022Article
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 2022Article
- Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity forFrontiers in cellular and infection microbiology · 2018Article
- Translational regulation of Yersinia enterocolitica mRNA encoding a type III secretion substrate.The Journal of biological chemistry · 2013Article
- Tetratricopeptide repeat motifs in the world of bacterial pathogens: role in virulence mechanisms.Infection and immunity · 2013Review
- Regulation of the Yersinia type III secretion system: traffic control.Frontiers in cellular and infection microbiology · 2013Review
- Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Microbiology and molecular biology reviews : MMBR · 2012Review
- YopD self-assembly and binding to LcrV facilitate type III secretion activity by Yersinia pseudotuberculosis.The Journal of biological chemistry · 2010Article
- Functional characterization of SsaE, a novel chaperone protein of the type III secretion system encoded by Salmonella pathogenicity island 2.Journal of bacteriology · 2009Article
- Control of gene expression by type III secretory activity.Current opinion in microbiology · 2008Review
- Structural characterization of the Yersinia pestis type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG.Journal of molecular biology · 2008Article
- Regulatory role of PopN and its interacting partners in type III secretion of Pseudomonas aeruginosa.Journal of bacteriology · 2007Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type III secretion systems are used by many animal and plant interacting bacteria to colonize their host. These systems are often composed of at least 40 genes, making their temporal and spatial regulation very complex. Some type III chaperones of the translocator class are important regulatory molecules, such as the LcrH chaperone of Yersinia pseudotuberculosis. In contrast, the highly homologous PcrH chaperone has no regulatory effect in native Pseudomonas aeruginosa or when produced in Yersinia. In this study, we used LcrH-PcrH chaperone hybrids to identify a discrete region in the N terminus of LcrH that is necessary for YscY binding and regulatory control of the Yersinia type III secretion machinery. PcrH was unable to bind YscY and the homologue Pcr4 of P. aeruginosa. YscY and Pcr4 were both essential for type III secretion and reciprocally bound to both substrates YscX of Yersinia and Pcr3 of P. aeruginosa. Still, Pcr4 was unable to complement a DeltayscY null mutant defective for type III secretion and yop-regulatory control in Yersinia, despite the ability of YscY to function in P. aeruginosa. Taken together, we conclude that the cross-talk between the LcrH and YscY components represents a strategic regulatory pathway specific to Yersinia type III secretion.
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