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Journal of Bacteriology, July 1999, p. 4012-4019, Vol. 181, No. 13
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Structure-Function Analysis of XcpP, a Component Involved in General Secretory Pathway-Dependent Protein Secretion in Pseudomonas aeruginosa

Sophie Bleves,dagger Manon Gérard-Vincent, Andrée Lazdunski, and Alain Filloux*

Laboratoire d'Ingéniérie des Systèmes Macromoléculaires, UPR9027, IBSM/CNRS, 13402 Marseille Cedex 20, France

Received 11 January 1999/Accepted 19 April 1999

The general secretory pathway of Pseudomonas aeruginosa is required for the transport of signal peptide-containing exoproteins across the cell envelope. After completion of the Sec-dependent translocation of exoproteins across the inner membrane and cleavage of the signal peptide, the Xcp machinery mediates translocation across the outer membrane. This machinery consists of 12 components, of which XcpQ (GspD) is the sole outer membrane protein. XcpQ forms a multimeric ring-shaped structure, with a central opening through which exoproteins could pass to reach the medium. Surprisingly, all of the other Xcp proteins are located in or are associated with the cytoplasmic membrane. This study is focused on the characteristics of one such cytoplasmic membrane protein, XcpP. An xcpP mutant demonstrated that the product of this gene is indeed an essential element of the P. aeruginosa secretion machinery. Construction and analysis of truncated forms of XcpP made it possible to define essential domains for the function of the protein. Some of these domains, such as the N-terminal transmembrane domain and a coiled-coil structure identified at the C terminus of XcpP, may be involved in protein-protein interaction during the assembly of the secretory apparatus.

* Corresponding author. Mailing address: Laboratoire d'Ingéniérie des Systèmes Macromoléculaires, UPR9027, IBSM/CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. Phone: (33) (0)491164127. Fax: (33) (0)491712124. E-mail: filloux{at}ibsm.cnrs-mrs.fr.

dagger Present address: Microbial Pathogenesis Unit, International Institute of Cellular and Molecular Pathology and Faculté de Médecine, Université Catholique de Louvain, B-1200 Brussels, Belgium.

Journal of Bacteriology, July 1999, p. 4012-4019, Vol. 181, No. 13
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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