Sen A, Todaro G J
Cell. 1977 Jan;10(1):91-9. doi: 10.1016/0092-8674(77)90143-x.
A structural protein purified from the Rous sarcoma virus (RSV) can specificially bind in vitro to purified avian, but not mammalian, type C viral RNA. Following ultraviolet irradiation of viral particles under conditions which stabilize the polyploid 70S viral RNA, the same polypeptide can be directly purified from the RSV genome. Based on its electrophoretic mobility in polyacrylamide gels containing sodium dodecylsulfate, the RNA binding protein has been identified as the major phosphoprotein (p19) of avian type C viruses. Similar experiments show that the major phosphoproteins of mammalian type C viruses (p12 for murine viruses and p16 for endogenous primate viruses) are also the specific RNA binding proteins and, similarly, are found closely associated with the 70S RNA genomes in the intact viral particles.
从劳氏肉瘤病毒(RSV)中纯化出的一种结构蛋白,在体外能特异性结合纯化的禽C型病毒RNA,而不能结合哺乳动物C型病毒RNA。在能稳定多倍体70S病毒RNA的条件下对病毒颗粒进行紫外线照射后,可直接从RSV基因组中纯化出相同的多肽。根据其在含十二烷基硫酸钠的聚丙烯酰胺凝胶中的电泳迁移率,该RNA结合蛋白已被鉴定为禽C型病毒的主要磷蛋白(p19)。类似实验表明,哺乳动物C型病毒的主要磷蛋白(鼠病毒的p12和内源性灵长类病毒的p16)也是特异性RNA结合蛋白,同样,在完整病毒颗粒中也发现它们与70S RNA基因组紧密相关。