title: Interaction domains in the Pseudomonas aeruginosa type II secretory apparatus component XcpS (GspF).
abstract: 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.
authors.affiliation: Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, the Netherlands.
authors.forename: Jorik
authors.initials: J
authors.lastname: Arts
authors.affiliation: 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.
authors.forename: Arjan
authors.initials: A
authors.lastname: de Groot
authors.affiliation: Laboratoire d'Ingénierie des Systèmes Macromoleculaires, UPR9027, IBSM/CNRS, 13402 Marseille Cedex 20, France.
authors.forename: Geneviève
authors.initials: G
authors.lastname: Ball
authors.affiliation: Laboratoire d'Ingénierie des Systèmes Macromoleculaires, UPR9027, IBSM/CNRS, 13402 Marseille Cedex 20, France.
authors.forename: Eric
authors.initials: E
authors.lastname: Durand
authors.affiliation: Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, the Netherlands.
authors.forename: Mohammed El
authors.initials: ME
authors.lastname: Khattabi
authors.affiliation: Laboratoire d'Ingénierie des Systèmes Macromoleculaires, UPR9027, IBSM/CNRS, 13402 Marseille Cedex 20, France.
authors.forename: Alain
authors.initials: A
authors.lastname: Filloux
authors.affiliation: Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, the Netherlands.
authors.forename: Jan
authors.initials: J
authors.lastname: Tommassen
authors.affiliation: Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, the Netherlands.
authors.forename: Margot
authors.initials: M
authors.lastname: Koster
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000378:metabolism; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D011550:Pseudomonas aeruginosa / Q000235:genetics / Q000378:metabolism*; D016958:Pseudomonas putida / Q000235:genetics; D011995:Recombination, Genetic
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; C082573:xcpR protein, Pseudomonas aeruginosa; C066761:xcpY protein, Pseudomonas aeruginosa