Expression of the Glutathione Synthetase Gene of Escherishia coli B in Saccharomyces cerevisiae

概要

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The coding region of the glutathione synthetase gene (gshII) of Escherichia coil was fused with the transcriptional signal of a promoter fragment (ΔP8) of Saccharomyces cerevisiae. The fused gshII (ΔP8-gshII) was expressed in S. cerevisiae and the expressed glutathione synthetase (GSH-II) was identical with that from E. coli in molecular weight and amino terminal sequence. Although the GSH-II activity in the transformant of S. cerevisiae increased more than 1,000-fold, the glutathione (GSH) production remained unchanged. The coexistence of the fused γ-glutamylcysteine synthetase gene (P8-gshI) with ΔP8-gshII in the hybrid plasmid pGSX120E caused the expression of both genes in S. cerevisiase and, consequently, an approximately 2.8-fold increase of GSH content was observed. These results suggest that the rate-limiting enzyme of GSH production in S. cerevisiae is γ-glutamylcysteine synthetase (GSH-I) rather than GSH-II, and that the concomitant enhancement of both GSH-I and GSH-II activities might be very effective for GSH hyperproduction.
社団法人日本生物工学会の論文
1989-12-25