PMID:14514681
| Citation |
Fux, L, Nussbaum-Shochat, A and Amster-Choder, O (2003) A fraction of the BglG transcriptional antiterminator from Escherichia coli exists as a compact monomer. J. Biol. Chem. 278:50978-84 |
|---|---|
| Abstract |
Expression of the bgl operon in Escherichia coli, induced by beta-glucosides, is positively regulated by BglG, a transcriptional antiterminator. In the presence of inducer, BglG dimerizes and binds to the bgl transcript to prevent premature termination of transcription. The dimeric state of BglG is determined by BglF, a membrane-bound enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system (PTS), which reversibly phosphorylates BglG according to beta-glucoside availability. BglG is composed of an RNA-binding domain followed by two homologous PTS regulation domains (PRD1 and PRD2). The predicted structure of dimeric LicT, a BglG homologue from Bacillus subtilis, suggests that the two PRDs adopt a similar structure and that the interactions within the dimer are PRD1-PRD1 and PRD2-PRD2. We have shown recently that the PRD1 and PRD2 domains of BglG can form a stable heterodimer. We report here, based on in vitro and in vivo cross-linking experiments, that a fraction of BglG is present in the cell in a compact form in which PRD1 and PRD2 are in close proximity. The compact form is present mainly in the BglG monomers. Our results imply that the monomer-dimer transition involves a conformational change. The possible role of the compact form in preventing untimely induction of the bgl operon is discussed. |
| Links |
PubMed Online version:10.1074/jbc.M308085200 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Cross-Linking Reagents; Cysteine; Dimerization; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Mutation; Operon; Protein Structure, Tertiary; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/genetics |
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