Escherichia coli tol and rcs genes participate in the complex network affecting curli synthesis.
Curli are necessary for the adherence of Escherichia coli to surfaces, and to each other, during biofilm formation, and the csgBA and csgDEFG operons are both required for their synthesis. A recent survey of gene expression in Pseudomonas aeruginosa biofilms has identified tolA as a gene activated in biofilms. The tol genes play a fundamental role in maintaining the outer-membrane integrity of Gram-negative bacteria. RcsC, the sensor of the RcsBCD phosphorelay, is involved, together with RcsA, in colanic acid capsule synthesis, and also modulates the expression of tolQRA and csgDEFG. In addition, the RcsBCD phosphorelay is activated in tol mutants or when Tol proteins are overexpressed. These results led the authors to investigate the role of the tol genes in biofilm formation in laboratory and clinical isolates of E. coli. It was shown that the adherence of cells was lowered in the tol mutants. This could be the result of a drastic decrease in the expression of the csgBA operon, even though the expression of csgDEFG was slightly increased under such conditions. It was also shown that the Rcs system negatively controls the expression of the two csg operons in an RcsA-dependent manner. In the tol mutants, activation of csgDEFG occurred via OmpR and was dominant upon repression by RcsB and RcsA, while these two regulatory proteins repressed csgBA through a dominant effect on the activator protein CsgD, thus affecting curli synthesis. The results demonstrate that the Rcs system, previously known to control the synthesis of the capsule and the flagella, is an additional component involved in the regulation of curli. Furthermore, it is shown that the defect in cell motility observed in the tol mutants depends on RcsB and RcsA.
Vianney
Anne
A
Unité de Microbiologie et Génétique, UMR5122 CNRS-INSA-UCBL, Université Claude Bernard Lyon1, bât A. Lwoff, 10, rue Dubois, 69622 Villeurbanne cedex, France.
Jubelin
Grégory
G
Unité de Microbiologie et Génétique, UMR5122 CNRS-INSA-UCBL, Université Claude Bernard Lyon1, bât A. Lwoff, 10, rue Dubois, 69622 Villeurbanne cedex, France.
Renault
Sophie
S
Unité de Microbiologie et Génétique, UMR5122 CNRS-INSA-UCBL, Université Claude Bernard Lyon1, bât A. Lwoff, 10, rue Dubois, 69622 Villeurbanne cedex, France.
Dorel
Corine
C
Unité de Microbiologie et Génétique, UMR5122 CNRS-INSA-UCBL, Université Claude Bernard Lyon1, bât A. Lwoff, 10, rue Dubois, 69622 Villeurbanne cedex, France.
Lejeune
Philippe
P
Unité de Microbiologie et Génétique, UMR5122 CNRS-INSA-UCBL, Université Claude Bernard Lyon1, bât A. Lwoff, 10, rue Dubois, 69622 Villeurbanne cedex, France.
Lazzaroni
Jean Claude
JC
Unité de Microbiologie et Génétique, UMR5122 CNRS-INSA-UCBL, Université Claude Bernard Lyon1, bât A. Lwoff, 10, rue Dubois, 69622 Villeurbanne cedex, France.
D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000096:biosynthesis*; D018441:Biofilms / Q000254:growth & development*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D029968:Escherichia coli Proteins / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D009097:Multienzyme Complexes / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D009097:Multienzyme Complexes; C489568:RcsB protein, E coli; D014157:Transcription Factors; C489728:rcsC protein, E coli; C067572:RcsA protein, E coli; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases