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The periplasmic binding protein of a tripartite tricarboxylate transporter is involved in signal transduction
- Source :
- Journal of molecular biology. 351(4)
- Publication Year :
- 2005
-
Abstract
- A new type of solute importer has been identified recently in various bacterial genera and called the tripartite tricarboxylate transporter (TTT). TTTs consist of two cytoplasmic membrane proteins and a periplasmic solute-binding protein. In the whooping cough agent Bordetella pertussis, a TTT system that has been called BctCBA mediates the uptake of citrate, with BctA and BctB being the membrane components and BctC, the periplasmic protein. Here, we describe that the expression of the bctCBA operon is induced by the presence of citrate in the milieu. The signalling cascade involves both BctC and the signal transduction two-component system BctDE, encoded by an operon adjacent to bctCBA. Furthermore, two-hybrid analyses and affinity chromatography experiments indicated that citrate-liganded BctC interacts with the periplasmic domain of the sensor protein, BctE. Thus, BctC is part of the signalling cascade leading to upregulation of the transporter operon in the presence of its solute, a new function for periplasmic binding proteins of TT transporters.
- Subjects :
- DNA, Bacterial
Operon
Recombinant Fusion Proteins
lac operon
Biology
Models, Biological
Bordetella pertussis
Citric Acid
Bacterial Proteins
Structural Biology
Two-Hybrid System Techniques
Molecular Biology
Base Sequence
Binding protein
Periplasmic space
Two-component regulatory system
Membrane protein
Biochemistry
Lac Operon
Periplasmic Binding Proteins
bacteria
Signal transduction
Carrier Proteins
Signal Transduction
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 351
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- Journal of molecular biology
- Accession number :
- edsair.doi.dedup.....21cc545f18c3e84dac8dcc987abd4ad7