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Interaction domains in the Pseudomonas aeruginosa type II secretory apparatus component XcpS (GspF)

Jorik Arts^1,

Arjan de Groot^1,2,,

Mohammed El Khattabi^1,

¹ Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, the Netherlands
² Laboratoire d'Ingénierie des Systèmes Macromoleculaires, UPR9027, IBSM/CNRS, 13402 Marseille Cedex 20, France

Correspondence
Margot Koster
M.C.Koster{at}bio.uu.nl

Pseudomonas aeruginosa is an opportunistic pathogen, which secretes a wide variety of enzymes and toxins into the extracellular medium. Most exoproteins are exported by the type II secretion machinery, the Xcp system, which encompasses 12 different proteins. One of the core components of the Xcp system is the inner-membrane protein XcpS (GspF), homologues of which can be identified in type II secretion machineries as well as in type IV piliation systems. In this study, XcpS was shown to be stabilized by co-expression of the XcpR (GspE) and XcpY (GspL) components of the machinery, demonstrating an interaction between these three proteins. By replacing segments of P. aeruginosa XcpS with the corresponding parts of its Pseudomonas putida counterpart, XcpS domains were identified that are important for species-specific functioning and thus represent putative interaction domains. The cytoplasmic loop of XcpS was found to be involved in the stabilization by XcpR and XcpY.

A table of oligonucleotides is available as supplementary data with the online version of this paper.

These authors contributed equally to this work.

Present address: Laboratoire d'Écologie Microbienne de la Rhizosphère, UMR 6191 CNRS-CEA-Université de la Mediterranée, DSV-DEVM, CEA Cadarache, F-13108 Saint-Paul-Lèz-Durance, France.

Present address: Department of Cellular Architecture and Dynamics, Utrecht University, 3584 CH Utrecht, the Netherlands.