Identification of XcpZ domains required for assembly of the secreton of Pseudomonas aeruginosa

Viviane Robert, Finbarr Hayes, Andrée Lazdunski, Gérard P F Michel

    Research output: Contribution to journalArticlepeer-review

    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.
    Original languageEnglish
    Pages (from-to)1779-1782
    Number of pages3
    JournalJournal of Bacteriology
    Volume184
    Issue number6
    DOIs
    Publication statusPublished - 2002

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