Protein cleavage during virus assembly: characterization of cleavage in T4 phage.
Protein cleavage during virus assembly: characterization of cleavage in T4 phage.
复制标题
病毒组装过程中的蛋白质裂解：T4 噬菌体中裂解的表征。
DOI：
10.1016/s0022-2836(75)80116-1
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发表时间：
1975
影响因子：
5.6
通讯作者：
M. Showe
中科院分区：
文献类型：
--
作者：
A. Tsugita;L. Black;M. Showe
自从报道了病毒前体蛋白在脊髓灰质炎病毒和T4噬菌体成熟过程中的裂解以来，许多动物和细菌病毒的生命周期中都有蛋白分解反应的报道。在T4噬菌体头部的成熟过程中，在十二烷基硫酸钠存在下，用聚丙烯酰胺凝胶电泳法显示了四种蛋白质，它们的流动性增加，表明分子量减少。它们是：P23，主要的衣壳蛋白，P24，次要的衣壳蛋白，IP-III和B1(或ALT)，成熟病毒粒子的内部蛋白。第五种蛋白质P22是病毒头部的核心成分，在脉冲追逐实验中从十二烷基硫酸钠凝胶中消失；推测它被切割成小片段(Hosoda&Levinthal，1968；Laemmli；1970；Kellenberger&Kellenberger-van der Kamp，1970；Dicksonet al.，1970；Coppoter al.1973)。Celiset等人(1973)证明，P23迁移率的降低是由于前体蛋白的切割，并导致前体的N-末端部分丢失。对于除P22外的所有T4前体蛋白，表面切割导致分子损失不到20%，其余80%完整地整合到病毒中。
Since the reports of cleavage of viron precursor proteins during the maturation of poliovirus and bacteriophage T4, proteolytic reactions have been reported during the life cycles of numerous animal and bacterial viruses. During the maturation of the head of bacteriophage T4, four proteins have been shown, by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate, to increase in mobility suggesting a decrease in molecular weight. They are: P23, the major capsid protein, P24, a minor capsid protein, IP-III and B1(or alt), internal proteins of the mature virion. A fifth protein, P22, a core component of the virus prohead, disappears from sodium dodecyl sulphate gels in pulse-chase experiments; presumably it is cleaved to small fragments (Hosoda & Levinthal, 1968; Laemmli; 1970; Kellenberger & Kellenberger-van der Kamp, 1970; Dicksonet al., 1970; Coppoet al., 1973). Celiset al.(1973) demonstrated that the reduction of mobility of P23 is due to cleavage of the precursor protein, and that it results in the loss of the N-terminal portion of the precursor. For all of the T4 precursor proteins excpet P22, the apparent cleavage results in the loss of less than 20% of the molecule, the remaining 80% being incorporated into the virus intact.