A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein.
A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein.
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DOI：
10.1073/pnas.78.2.1067
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发表时间：
1981-02
影响因子：
11.1
通讯作者：
H. Oppermann;W. Levinson;J. Bishop
中科院分区：
文献类型：
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作者：
H. Oppermann;W. Levinson;J. Bishop
一个单一的病毒蛋白（pp60src）介导的肿瘤转化的细胞感染劳氏肉瘤病毒。pp60src的免疫沉淀揭示了两种细胞蛋白（Mr 50，000和89，000），它们似乎以特定的方式与pp60src相关。这两种细胞蛋白都没有得到很好的表征，但人们认为两者都可能参与pp60src的功能。用非生理温度或某些化学试剂处理禽类细胞，以先前描述的果蝇的“热休克”反应的方式放大了几种蛋白质的产生。我们在这里报告，这些蛋白质之一，分子量为89，000，与pp60src相关的89千道尔顿蛋白质相同。89千道尔顿的蛋白质是未感染和感染细胞的主要成分，即使在没有诱导剂的情况下，但只有一小部分这种蛋白质似乎与劳氏肉瘤病毒转化的细胞中的pp60src相关。含有pp60src和89千道尔顿蛋白质的复合物可以通过仅涉及pp60src的免疫反应沉淀。89千道尔顿蛋白质的复合形式不直接与抗体反应，但在从复合物释放后恢复其反应性。我们的结论是，89千道尔顿的蛋白质结合pp60src在一个相对稳定的复合物。我们认为，89千道尔顿的蛋白质可能有重叠的作用，在病毒肿瘤发生和热休克反应，并在任何设置的蛋白质的功能的证据可能阐明其功能在其他。此外，它可能被证明是有益的，寻找其他重叠的细胞反应热休克和细胞的肿瘤转化pp60src。
A single viral protein (pp60src) mediates neoplastic transformation of cells infected with Rous sarcoma virus. Immunoprecipitation of pp60src has revealed two cellular proteins (Mr 50,000 and 89,000) that appear to associate with pp60src in a specific manner. Neither of the cellular proteins has been well characterized, but it is thought that both may participate in the function of pp60src. Treatment of avian cells with unphysiological temperature or certain chemical agents amplifies the production of several proteins in the manner of the "heat shock" response earlier described for Drosophila. We report here that one of these proteins, with a molecular weight of 89,000 is identical to the 89-kilodalton protein found associated with pp60src. The 89-kilodalton protein is a major constituent of both uninfected and infected cells, even in the absence of inducing agents, but only a small fraction of this protein appears to associate with pp60src in cells transformed by Rous sarcoma virus. The complex containing pp60src and the 89-kilodalton protein can be precipitated by an immune reaction involving pp60src alone. The complexed form of the 89-kilodalton protein did not react directly with antibodies but regained its reactivity subsequent to release from the complex. We conclude that the 89-kilodalton protein is bound to pp60src in a relatively stable complex. We suggest that the 89-kilodalton protein may have overlapping roles in viral oncogenesis and the heat shock response, and that evidence on the function of the protein in either setting may illuminate its function in the other. In addition, it may prove profitable to search for other overlaps between the cellular response to heat shock and the neoplastic transformation of cells by pp60src.