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Codon Bias-Adjusted BL21 Derivatives for Protein Expression

sing site-directed mutagenesis or by supplementing the host with extra copies of the cognate tRNA genes.

Now, Stratagene has generated BL21-CodonPlus-RIL chemically competent cells that carry extra copies of the argU, ileY, and leuW tRNA genes. The tRNAs encoded by these genes recognize the AGA/AGG, AUA, and CUA codons, respectively. To demonstrate their ability to facilitate the expression of heterologous recombinant genes that are only marginally expressed in conventional BL21 strains, BL21-CodonPlus(DE3)-RIL cells were transformed with vectors expressing genes fromhuman, yeast, and archaeal origins using the T7 RNA polymerase responsive promoter. IPTG-induced expression of all recombinant genes greatly increased in the BL21-CodonPlus(DE3)-RIL cells, compared to their expression in BL21-Gold(DE3) (Figure 1).

Fig.1

Expression of Difficult Proteins

To demonstrate the efficiency of BL21-CodonPlus-RIL cells to facilitate protein production in genes affected by poor codon usage, we compared the expression of a codon-adjusted form of the human cardiac troponin-T gene in conventional BL21-GoldDE3 cells (Figure 1,hcTnT-mut) with expression of the wild-type (hcTnT-wt) form in BL21-CodonPlus(DE3)-RIL cells. The expression of hcTnT in E. coli was previously shown to be solely restricted by the presence of two rare arginine codon pairs.4 This was demonstrated by synonymous replacement of the rare arginine codon pairs with frequently used arginine codons (hcTnT-mut), which results in efficient production of hcTnT-mut in E. coli. In Figure 1, BL21-CodonPlus(DE3)-RIL cells express hcTnT-wt at the same level observed for the codon-ad
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