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Protein secretion in Pseudomonas aeruginosa : characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase
Author(s) -
Bally Marc,
Filloux Alain,
Akrim Mohammed,
Ball Geneviéve,
Lazdunski Andree,
Tommassen Jan
Publication year - 1992
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1992.tb01550.x
Subject(s) - biology , pilus , biogenesis , gene , secretion , secretory protein , bacterial outer membrane , secretory pathway , signal peptide , atp binding cassette transporter , fimbria , genetics , peptide sequence , biochemistry , escherichia coli , transporter , cell , golgi apparatus
Summary 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 periptasm 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.