Amons R, Pluijms W, Roobol K, Möller W
FEBS Lett. 1983 Mar 7;153(1):37-42. doi: 10.1016/0014-5793(83)80115-x.
In the course of a structural analysis of the alpha-chain of elongation factor 1 from Artemia salina cysts, we present four amino acid sequences comprising together half of the polypeptide chain. A comparison of these sequences with the primary structure of elongation factor EF-Tu from Escherichia coli reveals a clear correspondence between the eukaryotic and prokaryotic protein throughout their polypeptide chains. The results support a basic conservation of the structure of the aminoacyl-tRNA carrying enzyme in evolution. The occurrence, in the eukaryotic factor, of several epsilon-trimethyllysine residues, is remarkable.
在对卤虫囊肿延伸因子1的α链进行结构分析的过程中,我们给出了四条氨基酸序列,它们共同构成了多肽链的一半。将这些序列与大肠杆菌延伸因子EF-Tu的一级结构进行比较,结果显示真核生物和原核生物蛋白质在整个多肽链上存在明显的对应关系。这些结果支持了氨酰-tRNA携带酶在进化过程中结构的基本保守性。真核生物因子中出现的几个ε-三甲基赖氨酸残基值得注意。