New Approach to Achieve High-Level Secretory Expression of Heterologous Proteins by Using Tat Signal Peptide
New Approach to Achieve High-Level Secretory Expression of Heterologous Proteins by Using Tat Signal Peptide
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利用Tat信号肽实现异源蛋白高水平分泌表达的新方法
DOI：
10.2174/092986609788490096
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发表时间：
2009-06-01
影响因子：
1.6
通讯作者：
Li, Yong-Quan
中科院分区：
文献类型：
--
作者：
Li, Yu-Dong;Zhou, Zhan;Li, Yong-Quan
双精氨酸转运（达特）途径是大肠杆菌分泌生产异源蛋白的一条有吸引力的途径。杆菌本研究探讨了沙门氏菌达特信号肽的潜在用途。以提高分泌表达。结果表明，达特信号肽（ssDagA）能有效地将活性绿色荧光蛋白（GFP）分泌到周质中。通过对信号序列稀有密码子的优化，GFP的表达量和分泌量提高了2-3倍。mRNA二级结构的不稳定性可以解释翻译速率的增加。总之，我们的策略可以提供一个新的方法，高水平分泌表达异源蛋白在E。杆菌
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.