Use of Rifampicin in T7 RNA Polymerase-Driven Expression of a Plant Enzyme. Rifampicin Improves Yield and Assembly.

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Authors

KUDEROVÁ Alena NANAK Elizabeth TRUKSA Martin BRZOBOHATÝ Břetislav

Year of publication 1999
Type Article in Periodical
Magazine / Source Protein Expression and Purification
MU Faculty or unit

Faculty of Science

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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