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Title 

Highly efficient secretion of heterologous proteins from Saccharomyces cerevisiae using inulinase signal peptides

Authors 

Bong Hyun ChungSoo Wan NamByung Moon KimYoung Hoon Park

Publisher 

Wiley-Blackwell

Issue Date 

1996

Citation 

Biotechnology and Bioengineering, vol. 49, no. 0, pp. 473-479

Keywords 

human interleukin-2human lipocortin- 1INU signal peptideMFα1 leader peptidesecretionpeptide synthesisprotein secretionsaccharomyces cerevisiaeInulinase signal peptidessaccharomyces

Abstract 

The INU genes of Kluyveromyces marxianus encode inulinases which are readily secreted from Saccharomyces cerevisiae into the culture medium. To evaluate the utility of the INU signal peptides for the secretion of heterologous proteins from S. cerevisiae, a variety of expression and secretion vectors were constructed with GAL 10 promoter and GAL7 terminator. The coding sequence for human lipocortin-1 (LC1) was inserted in-frame with the INU signal sequences, and then the secretion efficiency and localization of LC1 were investigated in more detail and compared with those when being expressed by the vector with the MFα1 leader peptide. The vector systems with INU signal peptides secreted ca. 95% of the total LC1 expressed into the extracellular medium, while the MFα1 leader peptide-containing vector resulted in very low secretion efficiency below 10%. In addition, recombinant human interleukin-2 (IL-2) was expressed and secreted with the vector systems with INU signal peptide, and a majority fraction of the human IL-2 expressed was found to be secreted into the extracellular medium as observed in LC1 expression.

ISSN 

0006-3592

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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