Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase

• Published in: Molecular microbiology Vol. 6; no. 9; p. 1121
• Main Authors: Bally, M, Filloux, A, Akrim, M, Ball, G, Lazdunski, A, Tommassen, J
• Format: Journal Article
• Language: English
• Published: England 01.05.1992
• Subjects: Amino Acid Sequence; Bacterial Proteins - metabolism; Base Sequence; DNA, Bacterial; Endopeptidases - genetics; Endopeptidases - metabolism; Escherichia coli - genetics; Genes, Bacterial; Genetic Complementation Test; Molecular Sequence Data; Mutation; Plasmids; Pseudomonas aeruginosa - genetics; Pseudomonas aeruginosa - metabolism; Sequence Homology, Nucleic Acid; Subcellular Fractions
• ISSN: 0950-382X
• DOI: 10.1111/j.1365-2958.1992.tb01550.x

The xcp genes are required for the secretion of most extracellular proteins by Pseudomonas aeruginosa. The products of these genes are essential for the transport of exoproteins across the outer membrane after they have reached the periplasm via a signal sequence-dependent pathway. To date, analysis of three xcp genes has suggested the conservation of this secretion pathway in many Gram-negative bacteria. Furthermore, the xcpA gene was shown to be identical to pilD, which encodes a peptidase involved in the processing of fimbrial (pili) subunits, suggesting a connection between pili biogenesis and protein secretion. Here the nucleotide sequences of seven other xcp genes, designated xcpR to -X, are presented. The N-termini of four of the encoded Xcp proteins display similarity to the N-termini of type IV pili, suggesting that XcpA is involved in the processing of these Xcp proteins. This could indeed be demonstrated in vivo. Furthermore, two other proteins, XcpR and XcpS, show similarity to the PilB and PilC proteins required for fimbriae assembly. Since XcpR and PilB display a canonical nucleotide-binding site, ATP hydrolysis may provide energy for both systems.