Succinate-mediated catabolite repression control on the production of glycine betaine catabolic enzymes in Pseudomonas aeruginosa PAO1 under low and elevated salinities - Archive ouverte HAL
Article Dans Une Revue Microbiology (Reading, England) Année : 2006

Succinate-mediated catabolite repression control on the production of glycine betaine catabolic enzymes in Pseudomonas aeruginosa PAO1 under low and elevated salinities

A. Bazire
D. Haras
  • Fonction : Auteur
Carlos Blanco

Résumé

Glycine betaine (GB) and its immediate precursors choline and carnitine, dimethylsulfonioacetate, dimethylsulfoniopropionate, ectoine and proline were effective osmoprotectants for Pseudomonas aeruginosa, but pipecolate, trehalose and sucrose had no osmoprotective effect. GB was accumulated stably or transiently when succinate or glucose, respectively, was used as a carbon and energy source. The catabolite repression mediated by succinate occurred at both low and high salinities, and it did not involve the global regulators Vfr and Crc. A proteomic analysis showed that at least 21 proteins were induced when GB was used as a carbon and energy source, and provided evidence that succinate repressed the synthesis of all these proteins. Many of the proteins induced by GB (sarcosine oxidase, serine hydroxymethyltransferase and serine dehydratase) are involved in GB catabolism. In addition, GB uptake was stimulated at high medium osmolalities but it was insensitive to catabolite repression by succinate. Despite its ability to inhibit betaine catabolism, succinate did not allow any better growth of P. aeruginosa cells under hyperosmotic constraint. Conversely, as observed for cells supplied with glucose, a transient accumulation of GB was sufficient to provide a significant cell osmoprotection

Dates et versions

hal-00023201 , version 1 (21-04-2006)

Identifiants

Citer

Farès Diab, Théophile Bernard, A. Bazire, D. Haras, Carlos Blanco, et al.. Succinate-mediated catabolite repression control on the production of glycine betaine catabolic enzymes in Pseudomonas aeruginosa PAO1 under low and elevated salinities. Microbiology (Reading, England), 2006, 152, pp.1395-406. ⟨10.1099/mic.0.28652-0⟩. ⟨hal-00023201⟩
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