Iatrou K, Tsitilou S G, Kafatos F C
Proc Natl Acad Sci U S A. 1984 Jul;81(14):4452-6. doi: 10.1073/pnas.81.14.4452.
We have previously shown that one type of high-cysteine silkmoth chorion protein (Hc-A) has evolved from the A family of chorion proteins by radical modifications of the NH2-terminal and COOH-terminal polypeptide arms: most of the arm sequences have been deleted, while short cysteine- and glycine-containing repeats have expanded into long arrays. Strikingly similar modifications of the arms have led to the evolution of a second type of high-cysteine protein (Hc-B) from the B family of chorion proteins. It appears that the parallel evolution of these high-cysteine-encoding gene families has not been entirely independent: examination of 3' untranslated regions shows evidence of information transfer between the two families.
我们之前已经表明,一种高半胱氨酸蚕蛾卵壳蛋白(Hc-A)是通过对NH2末端和COOH末端多肽臂进行彻底修饰,从卵壳蛋白的A家族进化而来的:大多数臂序列已被删除,而含半胱氨酸和甘氨酸的短重复序列已扩展成长阵列。臂的惊人相似修饰导致了第二种高半胱氨酸蛋白(Hc-B)从卵壳蛋白的B家族进化而来。这些高半胱氨酸编码基因家族的平行进化似乎并非完全独立:对3'非翻译区的检查显示了两个家族之间信息传递的证据。