RpoS-dependent stress tolerance in Pseudomonas aeruginosa

Article Abstract:

The human pathogen Pseudomonas aeruginosa is capable of surviving stressful conditions due to the alternative sigma factor encoded by the RpoS gene. This is evident in an experiment in which an rpoS mutant was synthesized to test the survival of Pseudomonas aeruginosa during exposure to high temperature, hyperosmolarity, hydrogen peroxide, low pH and ethanol. Results show that disruption of the rpoS gene led to a two- to threefold increase in the rate of kill of stationary-phase cells. It was deduced that factors other than the RpoS protein play a role in stationary-phase stress tolerance in Pseudomonas aeruginosa, as indicated by the higher stress resistance of stationary-phase cells of the RpoS-negative strain than exponentially growing RpoS-positive cells.

Pathogenic microorganisms, Genetic code

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The Pseudomonas aeruginosa tonB gene encodes a novel TonB protein

Article Abstract:

The Pseudomonas aeruginosa tonB gene encodes a 36,860 Da protein that is rich in Pro residues with Glu-Pro/Lys-Pro repeats. The P. aeruginosa TonB protein, TonB(sub P.a.) has no N-terminal membrane anchor sequence unlike other TonB proteins. An internal N-terminal signal/anchor sequence is, however, present. P. aeruginosa tonB derivatives lack siderophore-mediated iron acquisition and low iron supplies induce tonB expression. TonB(sub P.a.) is more similar to the Escherichia coli TonB protein than the P. putida protein.

Analysis, Amino acid sequence, Amino acid sequencing

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Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa

Article Abstract:

The role of the general secretory pathway (Gsp) protein termed XcpZ was examined in terms of stabilizing the components of the Xcp secretory apparatus in the Pseudomonas aeruginosa. GSP was considered the major pathway for the production of toxins and catabolic enzymes in P. aeruginosa. Using xcpZ mutants, it was discovered that a decrease in the XcpY amount was attributed to the absence of XcpZ and that XcpZ was absent in a xcpY mutant. XcpZ and XcpY directly interacted within the secretory apparatus.

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