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

• Published in: Microbiology (Society for General Microbiology) Vol. 144; no. 12; pp. 3379 - 3386
• Main Authors: Michel, Gerard, Bleves, Sophie, Ball, Genevieve, Lazdunski, Andree, Filloux, Alain
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.12.1998; Society for General Microbiology
• Subjects: Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacterial Proteins - physiology; Bacteriology; Biological and medical sciences; Escherichia coli - genetics; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Bacterial; Membrane Proteins; Membrane Transport Proteins; Microbiology; Mutation; Permeability, membrane transport, intracellular transport; Protein Binding; Pseudomonas aeruginosa; Pseudomonas aeruginosa - genetics; Pseudomonas aeruginosa - physiology; Pseudomonadales; Membrane protein; Structure stability; Transportation system; Secretion; Bacteria; Pseudomonadaceae; Molecular interaction; Pseudomonas aeruginosa; Molecular complex; Protein
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/00221287-144-12-3379

Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UPR9027, IBSM/CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France ABSTRACT Summary: 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. Author for correspondence: Gerard Michel. Tel: +33 491164487. Fax: +33 491712124. e-mail: michel@ibsm.cnrs-mrs.fr