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Expression of recombinant human inteleukin 6(rhIL6) in Saccharomyces cerevisiae by the midified phosphoglycerate kinase and chelatin promoter

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Abstract

Using the modified yeast expression vectors that contained phosphoglycerate kinase or chelatin promoter with the adenine (A) base at -3 position from the ATG coding sequences and the leu-2 gene, recombinant human interleukin-6 (rhIL-6) was produced as a β-galactosidase (lacZ) fusion protein in Saccharomyces cerevisiae. Expression level of the IL-6-lacZ was 12 times higher than that from the unmodified wild type plasmids and IL-6 activity was 9-9.8 x 105 unit/mg yeast total protein. Thus these modified yeast vectors are useful for high expression of foreign genes in yeast.

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