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Microbiology. 1998 Dec;144 ( Pt 12):3379-86.

Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa.

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Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UPR9027, IBSM/CNRS, Marseille, France.


Protein secretion in gram-negative bacteria is often dependent on the general secretory pathway (GSP). In Pseudomonas aeruginosa, this system requires at least 12 Xcp (Gsp) proteins, which are proposed to constitute a multiprotein complex localized in the bacterial envelope. Hitherto, little was known about the mutual interactions between Xcp proteins. In this study, mutants affected in the xcpZ gene encoding a bitopic inner-membrane protein were analysed to investigate the role of this protein in the architecture of the secretory machinery. The absence of XcpZ resulted in a decreased amount of XcpY. Reciprocally, XcpZ was not detectable in a xcpY mutant, demonstrating a mutual stabilization of these two proteins. These results strongly suggest that XcpZ and XcpY interact within the functional secretory apparatus.

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