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首页> 美国卫生研究院文献>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：猿猴病毒40基因A调节猿猴病毒40转化细胞中高度磷酸化的蛋白与染色质和核糖体之间的关联。

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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：十二烷基硫酸钠-聚丙烯酰胺凝胶电泳在体内或体外对这些蛋白进行磷酸化后，已比较了与猿猴病毒40（SV40）转化的和未转化的猴，小鼠和大鼠细胞的染色质和核糖体相关的蛋白种类。通过与这些细胞器相关的蛋白激酶和[γ- 32 P] ATP作为磷酰基供体进行体外磷酸化。反应产物含有大约相等量的磷酸丝氨酸和磷酸苏氨酸。磷酸化蛋白的电泳分析表明，分子量约为90,000的高度磷酸化的蛋白（90K蛋白）与转化细胞的染色质和核糖体有关，而与未转化细胞无关。可以使用0.5至1.0 M NaCl或KCl从染色质和核糖体中提取90K蛋白。 90K蛋白仍然与通过蛋白质合成系统中线粒体后上清液的嘌呤霉素反应制备的径流核糖体相关。 SV40 tsA转化的小鼠和大鼠细胞的染色质和核糖体的体外磷酸化表明，在限制性温度下培养细胞时，与这些细胞器相关的90K蛋白量大大减少。在用[ 3 标记的SV40 tsA转化的细胞制备的非组蛋白染色体和核糖体相关蛋白级分中，观察到了 32 P标记的90K蛋白量类似的温度依赖性降低。 sup> H]亮氨酸和[ 32 P]正磷酸盐体内。用高盐提取的非组蛋白染色体和核糖体相关蛋白中的体外磷酸化90K蛋白未用抗SV40 T血清免疫沉淀。

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