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首页> 外文期刊>Molecular and Cellular Biology >Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex.
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Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex.

机译：劳斯肉瘤病毒转化蛋白和两种细胞磷蛋白之间的相互作用：分析这种复合物的周转和分布。

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The transforming protein of Rous sarcoma virus (RSV), pp60src, was previously shown to associate with two cellular proteins of Mr 90,000 and 50,000 in RSV-transformed chicken cells. In this report, we demonstrate that this interaction is specific for a discrete population of pp60src molecules. Newly synthesized pp60src was found to preferentially associate with pp90 and pp50 to form a short-lived complex. The half-life of this complex varied from 9 to 15 min in cells transformed by nondefective strains of RSV. This interaction between pp60src, pp50, and pp90 took place in a soluble fraction of the cell, and the complex-bound pp60src molecules were not phosphorylated on tyrosine. These results suggest that pp90 and pp50 may be involved in the processing of pp60src molecules before the association of pp60src with the plasma membrane. The kinetics of dissociation of this complex were shown to be altered in cells infected with viruses containing a temperature-sensitive defect in the src gene. When cells infected with these viruses were grown at the nonpermissive temperature, more than 90% of the pp60src molecules were associated with pp90 and pp50, and little or no dissociation was observed in a 3-h chase period. These results suggest that mutations in the src gene which affect the transforming activity of pp60src also affect the stability of the interaction of pp60src with pp90 and pp50.
机译：先前已显示劳斯肉瘤病毒（RSV）的转化蛋白pp60src与RSV转化鸡细胞中的两种细胞蛋白90,000和50,000关联。在这份报告中，我们证明了这种相互作用是特定于pp60src分子离散种群的。发现新合成的pp60src优先与pp90和pp50缔合，形成短暂的复合物。在无缺陷的RSV菌株转化的细胞中，该复合物的半衰期从9到15分钟不等。 pp60src，pp50和pp90之间的这种相互作用发生在细胞的可溶级分中，并且与结合物结合的pp60src分子在酪氨酸上没有被磷酸化。这些结果表明，在pp60src与质膜结合之前，pp90和pp50可能参与了pp60src分子的加工。在感染了src基因中含有温度敏感缺陷的病毒的细胞中，这种复合物的分解动力学显示出改变。当感染了这些病毒的细胞在非允许温度下生长时，超过90％的pp60src分子与pp90和pp50相关，并且在3小时的追踪时间内几乎没有观察到解离。这些结果表明，影响pp60src转化活性的src基因突变也影响pp60src与pp90和pp50相互作用的稳定性。

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