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

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Title
An efficient genome-wide fusion partner screening system for secretion of recombinant proteins in yeast
Author(s)
Jung Hoon BaeBong Hyun Sung; Hyun-Jin Kim; Soon-Ho Park; Kwang Mook Lim; Mi Jin Kim; Cho-Ryong Lee; Jung Hoon Sohn
Bibliographic Citation
Scientific Reports, vol. 5, pp. 12229-12229
Publication Year
2015
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
Publisher
Springer-Nature Pub Group
DOI
http://dx.doi.org/10.1038/srep12229
Type
Article
Appears in Collections:
Division of Biomaterials Research > Synthetic Biology and Bioengineering Research Center > 1. Journal Articles
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