Secretion of human proteins from yeast:: stimulation by duplication of polyubiquitin and protein disulfide isomerase genes in Kluyveromyces lactis

The efficiency of secreted production of mammalian proteins from yeasts remain, unpredictably variable, depending on each protein. On the hypothesis that the control of protein conformation during protein translocation is the bottleneck in many cases, we examined the effects of an increased dosage of the genes coding for protein disulfide isomerase and of polyubiquitin on the secretion of two human proteins, serumalbumin and interleukin 1 beta. The yeast Kluyveromyces lactis was used as a production host. Duplication of either one of these genes had a strong stimulating effect on the production of the highly disulfide-bonded serumalbumin, but not of interleukin 1 beta. (C) 2001 Elsevier Science B.V. All rights reserved.