Imamura H, Jeon B, Wakagi T, Matsuzawa H
Department of Biotechnology, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo, Japan.
FEBS Lett. 1999 Sep 3;457(3):393-6. doi: 10.1016/s0014-5793(99)01081-9.
The Thermococcus litoralis 4-alpha-glucanotransferase (GTase) gene has a high content of AGA and AGG codons for arginine, which are extremely rare in Escherichia coli. Expression of the GTase gene in E. coli resulted in low protein production and the accumulation of inclusion bodies. However, simultaneous expression of GTase with tRNA(AGA), tRNA(AGG) and GroELS affected both the production and solubility of GTase, and production of soluble GTase increasing about 5-fold. This new E. coli expression system should be applicable to the expression of not only archaeal but also eukaryotic genes, which usually contain a large number of AGA and AGG codons.
嗜热栖热菌4-α-葡聚糖转移酶（GTase）基因中编码精氨酸的AGA和AGG密码子含量很高，而这些密码子在大肠杆菌中极为罕见。GTase基因在大肠杆菌中的表达导致蛋白质产量低且包涵体积累。然而，GTase与tRNA(AGA)、tRNA(AGG)和GroELS同时表达会影响GTase的产量和溶解性，可溶性GTase的产量增加了约5倍。这种新的大肠杆菌表达系统不仅应适用于古细菌基因的表达，也适用于通常含有大量AGA和AGG密码子的真核基因的表达。
