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- Title
Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase.
- Authors
Bally, Marc; Filloux, Alain; Akrim, Mohammed; Ball, Geneviève; Lazdunski, Andrée; Tommassen, Jan
- Abstract
The <em>xcp</em> genes are required for the secretion of most extracellular proteins by <em>Pseudomonas aeruginosa</em>. 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 <em>xcpA</em> gene was shown to be identical to <em>pilD</em>, 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 <em>xcpR</em> to -X, are presented. The <em>N</em>-termini of four of the encoded Xcp proteins display similarity to the <em>N</em>-termini of type IV pili, suggesting that XcpA is involved in the processing of these Xcp proteins. This could indeed be demonstrated <em>in vivo</em>. 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.
- Subjects
PSEUDOMONAS aeruginosa; GRAM-negative bacteria; PEPTIDASE; PILI (Microbiology); HYDROLYSIS
- Publication
Molecular Microbiology, 1992, Vol 6, Issue 9, p1121
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/j.1365-2958.1992.tb01550.x