Secretion of Escherichia coli beta-galactosidase in Saccharomyces cerevisiae using the signal sequence from the glucoamylase-encoding STA2 gene

Biochemical and Biophysical Research Communications
M VanoniL Alberghina

Abstract

The budding yeast Saccharomyces cerevisiae is a safe and widely used host for the production of recombinant DNA-derived proteins. We have used the signal sequence from the S. diastaticus STA2 gene, encoding glucoamylase II, to secrete Escherichia coli beta-galactosidase, encoded by the lacZ gene. In frame STA2/lacZ gene fusions have been constructed and expressed in S. cerevisiae under the control of either the STA2 or the galactose inducible GAL1-10 upstream promoters. Fairly high amounts of the enzyme (up to 76% of total activity, depending on the growth conditions) are secreted in the periplasmic space. Adding yeast extract and peptone to the growth medium results in a dramatic increase in both synthesis and secretion of beta-galactosidase.

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Citations

Apr 5, 1992·Biotechnology and Bioengineering·D PorroL Alberghina
Feb 18, 2011·Bioengineered Bugs·Lucília DominguesCarla Oliveira
Jan 1, 1991·Critical Reviews in Biochemistry and Molecular Biology·I S PretoriusJ Marmur
Jul 5, 2001·Protein Engineering·M BecerraM E Cerdán
Mar 15, 2020·Applied Microbiology and Biotechnology·Kristoffer Krogerus, Brian Gibson

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