Giannini G, Rappuoli R, Ratti G
Nucleic Acids Res. 1984 May 25;12(10):4063-9. doi: 10.1093/nar/12.10.4063.
The amino-acid sequences of two diphtheria toxin-related, non-toxic proteins, CRM45 and CRM197 , were deduced from the complete sequence of their genes: tox 45 and tox 197. CRM45 lacks the last 149 C-terminal amino-acid residues, but is otherwise identical to diphtheria toxin: a single C----T transition introduces an "ochre" (TAA) termination signal in tox 45, after the codon for threonine-386. A single G----A transition was also found in tox 197, leading to the substitution of glycine-52, present in the wild-type toxin, with glutamic acid in CRM197 . This aminoacid change is responsible for the loss of the NAD:EF2 ADP-ribosyltransferase activity in CRM197 , due most probably to an alteration of the NAD+ binding site.
两种与白喉毒素相关的无毒蛋白质CRM45和CRM197的氨基酸序列,是根据它们的基因tox 45和tox 197的完整序列推导出来的。CRM45缺少最后149个C末端氨基酸残基,但在其他方面与白喉毒素相同:一个C→T的转换在苏氨酸-386密码子之后的tox 45中引入了一个“赭石型”(TAA)终止信号。在tox 197中还发现了一个G→A的转换,导致野生型毒素中存在的甘氨酸-52被CRM197中的谷氨酸取代。这种氨基酸变化导致CRM197中NAD:EF2 ADP-核糖基转移酶活性丧失,很可能是由于NAD+结合位点的改变。