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

Bally, Marc; Filloux, Alain; Akrim, Mohammed; Ball, Genevève; Lazdunski, Andrée; Tommassen, Jan

doi:10.1111/j.1365-2958.1992.tb01452.x

Cited by 73 publications

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“…6 and 7 indicate relocalization of PulG upon the expression of other Pul secreton factors. This makes it unlikely that the secreton relocalizes the major pseudopilin to the OM, as was proposed previously (5).…”

Section: Discussionmentioning

confidence: 63%

Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System

et al. 2007

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The pseudopilin PulG is an essential component of the pullulanase-specific type II secretion system from Klebsiella oxytoca. PulG is the major subunit of a short, thin-filament pseudopilus, which presumably elongates and retracts in the periplasm, acting as a dynamic piston to promote pullulanase secretion. It has a signal sequence-like N-terminal segment that, according to studies with green and red fluorescent protein chimeras, anchors unassembled PulG in the inner membrane. We analyzed the early steps of PulG inner membrane targeting and insertion in Escherichia coli derivatives defective in different protein targeting and export factors. The ␤-galactosidase activity in strains producing a PulG-LacZ hybrid protein increased substantially when the dsbA, dsbB, or all sec genes tested except secB were compromised by mutations. To facilitate analysis of native PulG membrane insertion, a leader peptidase cleavage site was engineered downstream from the N-terminal transmembrane segment (PrePulG*). Unprocessed PrePulG* was detected in strains carrying mutations in secA, secY, secE, and secD genes, including some novel alleles of secY and secD. Furthermore, depletion of the Ffh component of the signal recognition particle (SRP) completely abolished PrePulG* processing, without affecting the Sec-dependent export of periplasmic MalE and RbsB proteins. Thus, PulG is cotranslationally targeted to the inner membrane Sec translocase by SRP.

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Section: Discussionmentioning

confidence: 63%

Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System

et al. 2007

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“…Since the lecB mutant was defective in type IV secretion, we examined whether the mutants also had defects in other secretion systems. In P. aeruginosa, the type II secretory pathway is used to export the largest number of proteins, including phospholipase C, alkaline protease, exotoxin A, LasA, and LasB (elastase) (3,4,16,19,23). We examined the proteolytic activities of lecA and lecB mutants by growing them on casein-milk agar plates.…”

Section: Fig 1 Proteomic Profile Of the Outer Membranes Of P Aerugmentioning

confidence: 99%

Pseudomonas aeruginosa LecB Is Involved in Pilus Biogenesis and Protease IV Activity but Not in Adhesion to Respiratory Mucins

2006

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Pseudomonas aeruginosa expresses two lectins which are implicated in adhesion and biofilm formation. In this study, we demonstrate that P. aeruginosa LecB is involved in pilus biogenesis and proteolytic activity. Moreover, neither lectin was involved in adhesion to human tracheobronchial mucin. We infer that some of the ascribed functions are secondary effects on other systems rather than effects of the lectins themselves.

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“…However, genetic analysis of the xcp cluster located at 40 min on the chromosome of P. aeruginosa revealed a different genetic organization. Nine xcp genes, xcpR to xcpZ, are arranged in a single operon structure, whereas xcpP and xcpQ are co-transcribed divergently with respect to the xcpR to xcpZ operon (Akrim et al, 1993;Bally et al, 1992;Filloux et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Regulation of the xcp secretion pathway by multiple quorum‐sensing modulons in Pseudomonas aeruginosa

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Akrim

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et al. 1997

Molecular Microbiology

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SummaryThe virulence of the opportunistic pathogen Pseudomonas aeruginosa is largely dependent upon the extracellular production of a number of secreted proteins with toxic or degradative activities. The synthesis of several exoenzymes is controlled in a cell-densitydependent manner by two interlinked quorum-sensing systems. Their secretion across the outer membrane occurs through the Xcp translocation machinery. The xcp locus located at 40 min on the chromosome consists of two divergently transcribed operons, namely xcpPQ and xcpR to xcpZ. In this study, transcriptional fusions were constructed between the xcpP and xcpR genes and the lacZ reporter. Transcriptional activation of the xcpP and xcpR genes in P. aeruginosa is growth-phase dependent and the lasR-lasI autoinduction system is required for this control. In the heterologous host Escherichia coli, the lasR gene product, together with its cognate autoinducer N-(3-oxododecanoyl)-L-homoserine lactone (OdDHL), activates both the xcpP-lacZ and the xcpR-lacZ gene fusion. The second P. aeruginosa quorum-sensing modulon rhlR-rhlI (vsmR-vsmI ) is also involved in the control of the xcp genes. Expression of the lacZ fusions is strongly reduced in PANO67, a pleiotropic mutant defective in the production of N-acyl-homoserine lactones responsible for the activation of RhlR. Furthermore, introduction of the lasR mutation in PANO67 results in additional diminution of xcpR transcription, indicating that the two systems can regulate their target genes independently. These data demonstrate that expression of the xcp secretion system depends on a complex regulatory network involving cell-cell signalling which controls production and secretion of virulence-associated factors.

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

Cited by 73 publications

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Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System

Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System

Pseudomonas aeruginosa LecB Is Involved in Pilus Biogenesis and Protease IV Activity but Not in Adhesion to Respiratory Mucins

Regulation of the xcp secretion pathway by multiple quorum‐sensing modulons in Pseudomonas aeruginosa

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