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J. Bacteriol. doi:10.1128/JB.01236-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II secretion system via the SRP/Sec pathway

Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, the Netherlands; Laboratoire d'Ingénierie des Systèmes Macromoleculaires, UPR9027, IBSM/CNRS, 13402 Marseille Cedex 20, France

^* To whom correspondence should be addressed. Email: M.C.Koster{at}uu.nl.

	Abstract

Type IV pilins and pseudopilins are found in various prokaryotic envelope protein complexes, including type IV pili and type II secretion machineries of Gram-negative bacteria, competence systems of Gram-positive bacteria, and flagella and sugar-binding structures within the archaeal kingdom. The precursors of these proteins have highly conserved N termini, consisting of a short positively charged leader peptide, which is cleaved off by a dedicated peptidase during maturation, and a hydrophobic stretch of approximately 20 amino acid residues. Which pathway is involved in the inner membrane translocation of these proteins is unknown. We used XcpT, the major pseudopilin from the type II secretion machinery of Pseudomonas aeruginosa, as a model to study this process. Transport of an XcpT-PhoA hybrid was shown to occur in the absence of other Xcp components in P. aeruginosa and in Escherichia coli. Experiments with conditional sec mutants and reporter-protein fusions showed that this transport process involves the co-translational SRP targeting route and is dependent on a functional Sec translocon.

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