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Title 

A novel fusion partner for enhanced secretion of recombinant proteins in Saccharomyces cerevisiae

 

효모에서 재조합 단백질 분비 증대를 위한 새로운 융합인자

Authors 

Jung Hoon BaeBong Hyun SungJeong-Woo SeoChul Ho KimJung Hoon Sohn

Publisher 

Springer Verlag (Germany)

Issue Date 

2016

Citation 

Applied Microbiology and Biotechnology, vol. 100, no. 0, pp. 10453-10461

Keywords 

Fusion partnerPurificationSaccharomyces cerevisiaeVOA1

Abstract 

Expressing proteins with fusion partners improves yield and simplifies the purification process. We developed a novel fusion partner to improve the secretion of heterologous proteins that are otherwise poorly excreted in yeast. The VOA1 (YGR106C) gene of Saccharomyces cerevisiae encodes a subunit of vacuolar ATPase. We found that C-terminally truncated Voa1p was highly secreted into the culture medium, even when fused with rarely secreted heterologous proteins such as human interleukin-2 (hIL-2). Deletion mapping of C-terminally truncated Voa1p, identified a hydrophilic 28-amino acid peptide (HL peptide) that was responsible for the enhanced secretion of target protein. A purification tag and a protease cleavage site were added to use HL peptide as a multi-purpose fusion partner. The utility of this system was tested via the expression and purification of various heterologous proteins. In many cases, the yield of target proteins fused with the peptide was significantly increased, and fusion proteins could be directly purified with affinity chromatography. The fusion partner was removed by in vitro processing, and intact proteins were purified by re-application of samples to affinity chromatography

ISSN 

0175-7598

Link 

http://dx.doi.org/10.1007/s00253-016-7722-2

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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