PMID:10200263
| Citation |
Nussbaum-Shochat, A and Amster-Choder, O (1999) BglG, the transcriptional antiterminator of the bgl system, interacts with the beta' subunit of the Escherichia coli RNA polymerase. Proc. Natl. Acad. Sci. U.S.A. 96:4336-41 |
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| Abstract |
The Escherichia coli BglG protein antiterminates transcription at two terminator sites within the bgl operon in response to the presence of beta-glucosides in the growth medium. BglG was previously shown to be an RNA-binding protein that recognizes a specific sequence located just upstream of each of the terminators and partially overlapping with them. We show here that BglG also binds to the E. coli RNA polymerase, both in vivo and in vitro. By using several techniques, we identified the beta' subunit of RNA polymerase as the target for BglG binding. The region that contains the binding site for BglG was mapped to the N-terminal region of beta'. The beta' subunit, produced in excess, prevented BglG activity as a transcriptional antiterminator. Possible roles of the interaction between BglG and the polymerase beta' subunit are discussed. |
| Links | |
| Keywords |
ATP-Binding Cassette Transporters; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Blotting, Western; Carrier Proteins/biosynthesis; Carrier Proteins/isolation & purification; Carrier Proteins/metabolism; Chromatography, Affinity; DNA-Directed RNA Polymerases/chemistry; DNA-Directed RNA Polymerases/isolation & purification; DNA-Directed RNA Polymerases/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Macromolecular Substances; Maltose-Binding Proteins; Monosaccharide Transport Proteins; Plasmids; RNA-Binding Proteins/isolation & purification; RNA-Binding Proteins/metabolism; Recombinant Fusion Proteins/biosynthesis; Recombinant Fusion Proteins/isolation & purification; Recombinant Fusion Proteins/metabolism; Sequence Deletion |
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