Dephosphorylation of the Escherichia coli Transcriptional Antiterminator BglG by the Sugar Sensor BglF Is the Reversal of Its Phosphorylation
| Autor: | Orna Amster-Choder, Qing Chen, Pieter W. Postma |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Phosphorylases
Recombinant Fusion Proteins Biology medicine.disease_cause Microbiology Dephosphorylation Phosphotransferase Glycogen phosphorylase Bacterial Proteins Escherichia coli Transcriptional regulation medicine Cysteine Phosphorylation Molecular Biology chemistry.chemical_classification Binding Sites Escherichia coli Proteins Membrane Proteins Methylglucosides RNA-Binding Proteins Active site Enzymes and Proteins Enzyme Models Chemical chemistry Biochemistry Mutation biology.protein Protein Kinases |
| Zdroj: | Journal of Bacteriology. 182:2033-2036 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | The Escherichia coli BglF protein catalyzes transport and phosphorylation of β-glucosides. In addition, BglF is a membrane sensor which reversibly phosphorylates the transcriptional regulator BglG, depending on β-glucoside availability. Therefore, BglF has three enzymatic activities: β-glucoside phosphotransferase, BglG phosphorylase, and phospho-BglG (BglG-P) dephosphorylase. Cys-24 of BglF is the active site which delivers the phosphoryl group either to the sugar or to BglG. To characterize the dephosphorylase activity, we asked whether BglG-P can give the phosphoryl group back to Cys-24 of BglF. Here we provide evidence which is consistent with the interpretation that Cys-24–P is an intermediate in the BglG-P dephosphorylation reaction. Hence, the dephosphorylation reaction catalyzed by BglF proceeds via reversal of the phosphorylation reaction. |
| Databáze: | OpenAIRE |
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