New Approach to Achieve High-Level Secretory Expression of Heterologous Proteins by Using Tat Signal Peptide

被引：11
|
作者：
Li, Yu-Dong [1 ]
Zhou, Zhan [1 ]
Lv, Long-Xian [1 ]
Hou, Xiao-Ping [1 ]
Li, Yong-Quan [1 ]
机构：
[1] Zhejiang Univ, Coll Life Sci, Hangzhou 310058, Zhejiang, Peoples R China
来源：
PROTEIN AND PEPTIDE LETTERS | 2009年 / 16卷 / 06期
关键词：
Twin-arginine translocation; codon usage; signal sequence; secretion; ARGININE TRANSLOCATION PATHWAY; GREEN FLUORESCENT PROTEIN; ESCHERICHIA-COLI; STREPTOMYCES-COELICOLOR; SECONDARY STRUCTURE; CODON USAGE; EXPORT; SEQUENCES; LOCALIZATION; PREDICTION;
D O I：
10.2174/092986609788490096
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The twin-arginine translocation (Tat) pathway is an attractive route for secretory production of heterologous proteins in E. coli. In this study, we investigated the potential use of Tat signal peptide from S. coelicolor to improve secretory expression. The results showed that Tat signal peptide (ssDagA) could effectively secrete active Green fluorescent protein (GFP) to periplasm. When the rare codons of signal sequence were optimized, the expression and secretion yield of GFP improved by about 2-3 folds as detected qualitatively by western blotting and fluorescent analysis. The increase of translation rate could be explained by the unstability of mRNA secondary structure. In summary, our strategy could provide a new approach for high-level secretory expression of heterologous proteins in E. coli.
引用
收藏
页码：706 / 710
页数：5
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