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Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
Published on: February 24, 2026
Improved membrane protein expression in Lactococcus lactis by fusion to Mistic
Yi Xu1, Jian Kong1, Wentao Kong2,1
1State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong Province, China.
Microbiology (Reading, England)
|March 23, 2013
Summary
Researchers developed a novel system in Lactococcus lactis for overexpressing difficult membrane proteins. This Mistic chaperoning strategy achieved high yields for both eukaryotic and prokaryotic proteins, enabling functional studies.
Area of Science:
- Microbiology
- Biotechnology
- Protein Expression
Background:
- Overexpressing membrane proteins for research is challenging.
- Lactococcus lactis offers advantages for membrane protein production.
Purpose of the Study:
- To establish a novel membrane protein expression system in L. lactis.
- To investigate the efficacy of the Mistic chaperoning strategy for high-yield protein production.
Main Methods:
- Introduction of the Mistic peptide into L. lactis to create a new expression system.
- Overexpression of a eukaryotic membrane protein (pkjDes4) and a prokaryotic membrane protein (pkjLi).
- Characterization of the functionality of the expressed pkjLi enzyme.
Main Results:
- Achieved high expression levels: 4.4% for pkjDes4 and 45.2% for pkjLi.
- Demonstrated robust production of both eukaryotic and prokaryotic membrane proteins.
- Confirmed functionality of expressed pkjLi, producing 0.852 mg/ml conjugated linoleic acid.
Conclusions:
- Successfully established a functional membrane protein expression system in L. lactis.
- The Mistic chaperoning strategy facilitates high-yield production of challenging membrane proteins.
- This system shows extraordinary capacity for producing intractable membrane proteins.
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