Sen A, Sherr C J, Todaro G J
Cell. 1977 Mar;10(3):489-96. doi: 10.1016/0092-8674(77)90036-8.
The purified p12 phosphoprotein of Rauscher murine leukemia virus was fractionated by ion exchange chromatography into subpopulations of molecules containing different amounts of covalently linked phosphate. Of the various phosphorylated forms of p12 protein purified from virions, only a species containing relatively little phosphate can bind in vitro to purified homologous 70S viral RNA. Using ultraviolet irradiation to stabilize ribonucleoprotein complexes in intact virions, the same molecular species of p12 phosphoprotein can be isolated in close association with the 70S viral genome. The results show that phosphorylation of type C viral p12 proteins influences the extent, but not the specificity, of their interaction with homologous viral RNA.
劳氏鼠白血病病毒纯化的p12磷蛋白通过离子交换色谱法分离成含有不同共价连接磷酸量的分子亚群。从病毒粒子中纯化的p12蛋白的各种磷酸化形式中，只有一种含磷相对较少的分子能在体外与纯化的同源70S病毒RNA结合。利用紫外线照射稳定完整病毒粒子中的核糖核蛋白复合物，可分离出与70S病毒基因组紧密结合的相同分子种类的p12磷蛋白。结果表明，C型病毒p12蛋白的磷酸化影响其与同源病毒RNA相互作用的程度，但不影响其特异性。
