Bouadloun F, Donner D, Kurland C G
Department of Molecular Biology, University of Uppsala, Sweden.
EMBO J. 1983;2(8):1351-6. doi: 10.1002/j.1460-2075.1983.tb01591.x.
We have developed a simple method for measuring the missense substitution of amino acids at specified positions in proteins synthesized in vivo. We find that the frequency of cysteine substitution for the single arginine in Escherichia coli ribosomal protein L7/L12 is close to 10(-3) for wild-type bacteria, decreases to 4 x 10(-4) in streptomycin-resistant bacteria containing mutant S12 (rpsL), and is virtually unchanged in Ram bacteria containing mutant S4 (rpsD). We have also found that the frequency of the cysteine substitution for the single tryptophan in E. coli ribosomal protein S6 is 3-4 x 10(-3) for wild-type bacteria, decreases to 6 x 10(-4) in streptomycin-resistant bacteria and is elevated to nearly 10(-2) in Ram bacteria.
我们开发了一种简单的方法,用于测量在体内合成的蛋白质中特定位置氨基酸的错义替换。我们发现,对于野生型细菌,大肠杆菌核糖体蛋白L7/L12中单个精氨酸被半胱氨酸取代的频率接近10^(-3),在含有突变体S12(rpsL)的链霉素抗性细菌中降至4×10^(-4),而在含有突变体S4(rpsD)的Ram细菌中几乎没有变化。我们还发现,对于野生型细菌,大肠杆菌核糖体蛋白S6中单个色氨酸被半胱氨酸取代的频率为3 - 4×10^(-3),在链霉素抗性细菌中降至6×10^(-4),而在Ram细菌中升高至近10^(-2)。