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首页> 外文期刊>Journal of Virology >Simian Virus 40 Gene A Regulates the Association Between a Highly Phosphorylated Protein and Chromatin and Ribosomes in Simian Virus 40-Transformed Cells
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Simian Virus 40 Gene A Regulates the Association Between a Highly Phosphorylated Protein and Chromatin and Ribosomes in Simian Virus 40-Transformed Cells

机译：Simian病毒40基因A调节在Simian病毒40转化细胞中高磷酸化的蛋白质和染色质和核糖体之间的关联

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摘要

The species of proteins associated with chromatin and ribosomes of simian virus 40 (SV40)-transformed and untransformed monkey, mouse, and rat cells have been compared by sodium dodecyl sulfate-polyacrylamide gel electrophoresis after phosphorylation of these proteins either in vivo or in vitro. In vitro phosphorylation was carried out by protein kinase associated with these organelles and [γ-32 P]ATP as the phosphoryl donor. The reaction products contained both phosphoserine and phosphothreonine in approximately equal amounts. The electrophoretic analysis of the phosphorylated proteins revealed that the highly phosphorylated protein with a molecular weight of approximately 90,000 (90K protein) was associated with chromatin and ribosomes from transformed cells but not from untransformed cells. The 90K protein could be extracted from chromatin and ribosomes with 0.5 to 1.0 M NaCl or KCl. The 90K protein was still associated with the runoff ribosomes prepared by the puromycin reaction of the post-mitochondrial supernatant in the protein-synthesizing system. In vitro phosphorylation of chromatin and ribosomes from SV40 tsA-transformed mouse and rat cells indicated that the amounts of 90K protein associated with these organelles decreased greatly when the cells were cultivated at the restrictive temperature. A similar temperature-dependent decrease in the amount of 32P-labeled 90K protein was observed in nonhistone chromosomal and ribosome-associated protein fractions prepared from SV40 tsA-transformed cells labeled with [3H]leucine and [32P]orthophosphate in vivo. In vitro phosphorylated 90K protein in nonhistone chromosomal and ribosome-associated proteins extracted with high salt was not immunoprecipitated with anti-SV40 T sera.
机译：通过在体内或体外磷酸化后，通过十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳比较了与染色体病毒40（SV40） - 转化和未转化的猴子，小鼠和大鼠细胞相关的蛋白质的种类。体外磷酸化通过与这些细胞器相关的蛋白激酶和[γ- 32/13> p] ATP作为磷素供体进行。反应产物含有大约相等的量磷素和磷酸磷酸萘。磷酸化蛋白的电泳分析显示，具有约90,000（90k蛋白）的分子量的高磷酸化蛋白与来自转化细胞的染色质和核糖体，但不是来自未转化的细胞。可以从染色质和核糖体中提取90k蛋白，其中0.5-1.0m NaCl或Kcl。 90k蛋白仍然与通过在蛋白质合成系统中的线粒体上上清液的嘌呤霉素反应制备的径向核糖体相关。从SV40 TSA-Transformed小鼠和大鼠细胞的体外磷酸化和来自SV40 -Transformed小鼠和大鼠细胞的磷酸酯表明，当细胞在限制温度下培养细胞时，与这些细胞器相关的90K蛋白质的量大大降低。在由SV40 TSA-Transformed细胞中制备的非甾铬染色体和核糖体相关蛋白质级分中观察到类似的温度依赖性降低 32-sup> p标记的90k蛋白质。 [ 3 h]亮氨酸和[ 32 p]正磷酸盐。用抗SV40 T血清免疫沉淀的非甾脂染色体和核糖体相关蛋白质中的体外磷酸化90K蛋白质。

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