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• W1984926939 abstract "Abstract Expression of the bgl operon in Escherichia coli, induced by β-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 β-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." @default.
• W1984926939 created "2016-06-24" @default.
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• W1984926939 date "2003-12-01" @default.
• W1984926939 modified "2023-09-29" @default.
• W1984926939 title "A Fraction of the BglG Transcriptional Antiterminator from Escherichia coli Exists as a Compact Monomer" @default.
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• W1984926939 doi "https://doi.org/10.1074/jbc.m308085200" @default.
• W1984926939 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14514681" @default.
• W1984926939 hasPublicationYear "2003" @default.
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