Mapping of a YscY binding domain within the LcrH chaperone that is required for regulation of Yersinia type III secretion
2005 (English)In: Journal of Bacteriology, ISSN 0021-9193, E-ISSN 1098-5530, Vol. 187, no 22, 7738-7752 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
American Society for Microbiology , 2005. Vol. 187, no 22, 7738-7752 p.
Amino acid sequence, bacterial proteins, binding sites, DNA; bacterial, HeLa cells, humans, molecular chaperones, molecular sequence data, protein interaction mapping, protein structure; tertiary, protein transport, sequence analysis; DNA, Yersinia pseudotuberculosis
IdentifiersURN: urn:nbn:se:umu:diva-16672DOI: 10.1128/JB.187.22.7738-7752.2005ISI: 000233400200021PubMedID: 16267298OAI: oai:DiVA.org:umu-16672DiVA: diva2:156345