期刊
SCIENTIFIC REPORTS
卷 5, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/srep12229
关键词
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资金
- Global Frontier Program of Korea Ministry of Science, ICT, and Future Planning [2010-0029737]
- Agri-Bioindustry Technology Development Program of Ministry of Agriculture, Food, and Rural Affairs
- R&D Convergence Program of National Research Council of Science Technology [171-102-1789]
- Research Initiative Program of KRIBB
- National Research Foundation of Korea [2010-0029737] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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 mgq/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 gq/L. This screening technique could provide new methods for the production of various types of difficult-to-express proteins.
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