Article
2-Methylcitrate-dependent activation of the propionate catabolic operon (prpBCDE) of Salmonella enterica by the PrpR protein.
Microbiology (Reading, England) - 1 Nov 2004
Palacios Sergio, Escalante-Semerena Jorge C
Abstract excerpt
The function of the PrpR protein of Salmonella enterica serovar Typhimurium LT2 was studied in vitro and in vivo. The PrpR protein is a sensor of 2-methylcitrate (2-MC), an intermediate of the 2-methylcitric acid cycle used by this bacterium to convert propionate to pyruvate. PrpR was unresponsive to citrate (a close structural analogue of 2-MC) and to propionate, suggesting that 2-MC, not propionate, is the...
Topics
- Adaptation, Physiological
- Adenosine Triphosphatases
- Bacterial Proteins
- Citrates
- DNA Footprinting
- DNA Mutational Analysis
- DNA-Binding Proteins
- Enzyme Activators
- Gene Expression Regulation, Bacterial
- Mutation
- Operon
- Promoter Regions, Genetic
- Propionates
- Protein Binding
- Protein Structure, Tertiary
- Salmonella typhimurium
- Signal Transduction