Identification of XcpZ domains required for assembly of the secreton of Pseudomonas aeruginosa.
Most of the exoproteins secreted by Pseudomonas aeruginosa are transported via the type II secretion system. This machinery, which is widely conserved in gram-negative bacteria, consists of 12 Xcp proteins organized as a multiprotein complex, also called the secreton. We previously reported that the mutual stabilization of XcpZ and XcpY plays an important role in the assembly of the secreton. In this study, we engineered variant XcpZ proteins by using linker insertion mutagenesis. We identified three distinct regions of XcpZ required for both the stabilization of XcpY and the functionality of the secreton. Interestingly, we also demonstrated that another component of the machinery, XcpP, can modulate the stabilizing activity of XcpZ on XcpY.
Robert
Viviane
V
Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, CNRS, 13402 Marseille Cedex 20, France.
Hayes
Finbarr
F
Lazdunski
Andrée
A
Michel
Gérard P F
GP
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001692:Biological Transport; D015964:Gene Expression Regulation, Bacterial; D005816:Genetic Complementation Test; D015151:Immunoblotting; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D011550:Pseudomonas aeruginosa / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000032:analysis / Q000378:metabolism
D001426:Bacterial Proteins; D008565:Membrane Proteins; C066762:xcpZ protein, Pseudomonas aeruginosa; D012697:Serine Endopeptidases; C104058:xanthomonapepsin