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利用Sanger双脱氧链终止法对黄羽扇豆（Lupinusluteus）翻译延伸因子2（EF2）的全长cDNA克隆进行了序列分析。该cDNA长度为2794bp,其中包括5’末端的80bp非翻译区,3’末端185bp非翻译区和2529bp长编码序列,3’末端为一18bp poly（A）尾。与其它GTP结合蛋白比较其编译的843aa（氨基酸）序列,发现它们具有显著的同源性;黄羽扇豆EF2与甜菜EF2的氨基酸序列90％相同。其差异主要存在于序列的中部;而与肽基tRNA和核糖体作用部位、与GTP结合部位和GTP酶活性有关的部位具有很高的保守性。黄羽扇豆EF2第700个氨基酸残基组氨酸是白喉毒素的ADP-核糖基化部位。
The full-length cDNA clone of translation extension factor 2 (EF2) from Lupus erythematosus was sequenced by Sanger dideoxy chain termination method. The cDNA was 2794bp in length, including the 80bp untranslated region at the 5 ’end, the 185bp untranslated region at the 3’ end and the 2529bp long coding sequence, and an 18bp poly (A) tail at the 3 ’end. Their 843aa (amino acid) sequences were compared to other GTP binding proteins and found to have significant homology; the amino acid sequence of yellow lupine EF2 was 90% identical to that of sugar beet EF2. The difference mainly exists in the middle part of the sequence, but it is highly conserved with the sites of peptidyl tRNA and ribosome interaction, GTP binding site and GTPase activity. Yellow Lupine EF2 The 700th amino acid residue Histidine is the ADP-ribosylation site of diphtheria toxin.