Bonatti S, Blobel G
J Biol Chem. 1979 Dec 25;254(24):12261-4.
Partial NH2-terminal sequence analysis has been performed on some products that result from the translation of 26 S mRNA of Sindbis virus either in vivo or in vitro. In vivo products were obtained after pulse-labeling of virus-infected cells. In vitro products were obtained after cell-free translation either in the absence or presence of microsomal membrane vesicles from dog pancreas. The sequence data indicate that the selective translocation across the microsomal membrane required for a distinct portion of one of the integral viral envelope proteins (PE2) is not accompanied by cleavage of its putative signal sequence. Furthermore, the NH2-terminal sequence of a proteolytic derivative (PE'2) that contains the bulk of PE2 and that is generated after exposure of the microsomal vesicles to proteolytic enzymes is identical to that of intact PE2, strongly suggesting that only a COOH-terminal portion of PE2 is excluded from translocation across the microsomal membrane.
已对辛德毕斯病毒26S mRNA在体内或体外翻译产生的一些产物进行了部分氨基末端序列分析。体内产物是在对病毒感染细胞进行脉冲标记后获得的。体外产物是在无细胞翻译后获得的，无细胞翻译是在不存在或存在来自狗胰腺的微粒体膜泡的情况下进行的。序列数据表明，完整病毒包膜蛋白之一（PE2）的一个不同部分跨微粒体膜的选择性易位并不伴随着其假定信号序列的切割。此外，一种蛋白水解衍生物（PE'2）的氨基末端序列与完整PE2的相同，该衍生物包含大部分PE2，是在微粒体泡暴露于蛋白水解酶后产生的，这强烈表明只有PE2的羧基末端部分被排除在跨微粒体膜的易位之外。
