Use of Rifampicin in T7 RNA Polymerase-Driven Expression of a Plant Enzyme. Rifampicin Improves Yield and Assembly.
| Authors | |
|---|---|
| Year of publication | 1999 |
| Type | Article in Periodical |
| Magazine / Source | Protein Expression and Purification |
| MU Faculty or unit | |
| Citation | |
| Field | Genetics and molecular biology |
| Keywords | rifampicin - protein expression - T7 RNA polymerase - beta-glucosidase |
| Description | Expression systems based on high selectivity and activity of T7 RNA polymerase and presence of a strong T7 promoter have been commonly used for cloning and expression of various recombinant proteins in Escherichia coli. When protein expression is not directed to periplasm, the final yield and quality of the synthesized and purified protein then depend on various factors, protein size, amino acid sequence, solubility in cytoplasm, and folding requirements among them. The yield in the T7 RNA polymerase/promoter system can be positively influenced by use of rifampicin. In this report we describe rifampicin-enhaced expression of a plant cytokinin-specific beta-glucosidase. The antibiotic not only increased the yield of the recombinant protein, which seems to be a general phenomenon, but also favored the final assembly of the protein's subunits into a catalytically active dimer form. |
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