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Title 

An efficient genome-wide fusion partner screening system for secretion of recombinant proteins in yeast

Authors 

Jung Hoon BaeBong Hyun SungHyun-Jin KimSoon-Ho ParkKwang Mook LimMi Jin KimCho-Ryong LeeJung Hoon Sohn

Publisher 

Nature Publishing Group

Issue Date 

2015

Citation 

Scientific Reports, vol. 5, no. 0, pp. 12229-12229

Abstract 

To produce rarely secreted recombinant proteins in the yeast Saccharomyces cerevisiae, we developed a novel genome-wide optimal translational fusion partner (TFP) screening system that involves recruitment of an optimal secretion signal and fusion partner. A TFP library was constructed from a genomic and truncated cDNA library by using the invertase-based signal sequence trap technique. The efficiency of the system was demonstrated using two rarely secreted proteins, human interleukin (hIL)-2 and hIL-32. Optimal TFPs for secretion of hIL-2 and hIL-32 were easily selected, yielding secretion of these proteins up to hundreds of mg/L. Moreover, numerous uncovered yeast secretion signals and fusion partners were identified, leading to efficient secretion of various recombinant proteins. Selected TFPs were found to be useful for the hypersecretion of other recombinant proteins at yields of up to several g/L. This screening technique could provide new methods for the production of various types of difficult-to-express proteins.

ISSN 

2045-2322

Link 

http://dx.doi.org/10.1038/srep12229

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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