Arrigo A P, Darlix J L, Spahr P F
Department of Pathology, University of Colorado Health Sciences Center, Denver 80262, USA.
EMBO J. 1983;2(3):309-15. doi: 10.1002/j.1460-2075.1983.tb01424.x.
In chick embryo fibroblasts transformed by Rous sarcoma virus (RSV) the tyrosine phosphorylation of a cellular protein of 34,000 daltons mol. wt. (34 kd) is greatly enhanced; this was shown to be catalyzed by the phosphotransferase activity of RSV transforming protein pp60src. We report here that in cytoplasmic extracts of both normal and transformed cells, in the presence of magnesium ions, the majority of the 34-kd protein is associated with large structures and that a fraction of 34 kd appears to be associated with ribonucleoprotein particles (RNPs). In addition, upon u.v. light cross-linking of RNA to protein in normal or transformed cells, an anti-34 kd serum immunoprecipitates RNA fragments of apparent low sequence complexity as detected by T1 fingerprint analysis. Our results indicate that the 34-kd protein may play a role in the cell at the level of RNPs.
在被劳氏肉瘤病毒（RSV）转化的鸡胚成纤维细胞中，一种分子量为34,000道尔顿（34kd）的细胞蛋白的酪氨酸磷酸化显著增强；已证明这是由RSV转化蛋白pp60src的磷酸转移酶活性催化的。我们在此报告，在正常细胞和转化细胞的细胞质提取物中，在镁离子存在的情况下，大部分34kd蛋白与大的结构相关联，并且一部分34kd似乎与核糖核蛋白颗粒（RNP）相关联。此外，在正常细胞或转化细胞中经紫外线使RNA与蛋白质交联后，一种抗34kd血清免疫沉淀出经T1指纹分析检测显示序列复杂性明显较低的RNA片段。我们的结果表明，34kd蛋白可能在细胞中RNP水平发挥作用。
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