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首页> 外文期刊>Journal of Virology >Stabilization of the large T protein in temperature-independent (type A) FR 3T3 rat cells transformed with the simian virus 40 tsA30 mutant.
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Stabilization of the large T protein in temperature-independent (type A) FR 3T3 rat cells transformed with the simian virus 40 tsA30 mutant.

机译：用硅藻病毒40 TSA30突变体转化的温度无关（A型）FR 3T3大鼠细胞的大T蛋白质的稳定化。

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The stabilities of in vivo [35S]methionine-labeled large T and small t proteins, synthesized in temperature-sensitive (type N) and temperature-insensitive (type A) FR 3T3 rat cells transformed by an early temperature-sensitive mutant of simian virus 40 (SV40), tsA30, were analyzed at the permissive and restrictive temperatures. The two polypeptides, detected in greatly reduced amounts in cells of the N type at the restrictive temperature, were also unstable at the permissive temperature. However, both were made in similar amounts and were apparently stable in cells of the A type, irrespective of the temperature. The structures of the viral RNAs present at the permissive temperature were analyzed for transformants representative of each type, and containing a single integration of viral DNA. The two cell lines synthesized transcripts identical to the large T and small t mRNAs identified in SV40-infected monkey cells. Similar amounts of viral RNA were found in A and N transformants in active growth at the permissive and restrictive temperatures, which argued against a control at a transcriptional level. Assay of a defined function of the protein, namely, the binding of nucleotide detected by affinity labeling with periodate-oxidized [alpha-32P]ATP, clearly showed that the large T proteins from both types of transformants exhibited, at least for that particular biochemical function, the same in vitro temperature sensitivity. In transformants of the A type only could a reduced binding activity be detected in extracts from cells grown at the restrictive temperature. Thus, the temperature-independent behavior of the A transformants may result from an in vivo partial stabilization of the newly synthesized large T protein, probably through interaction with a cellular component(s).
机译：体内[35s]甲硫氨酸标记的大型T和小T蛋白的稳定性，由Simian病毒的早期温度敏感突变体转化为温度敏感（n型）和温度不敏感（A型）FR 3T3大鼠细胞。在允许和限制温度下分析40（SV40）TSA30。在限制温度下，在N型N型细胞中检测到的两种多肽在允许温度下也不稳定。然而，两者都以相似的量制备，并且在A型的细胞中显然是稳定的，而不管温度如何。针对各种类型的转化体分析存在于允许温度下的病毒RNA的结构，并含有病毒DNA的单一整合。两种细胞系合成转录物与SV40感染的猴细胞中鉴定的大T和小T mRNA相同。在A和N转化体中发现类似量的病毒RNA，其在允许和限制温度下的活性生长中，其在转录水平上涉及对照。测定蛋白质的定义功能，即通过亲和标记检测的核苷酸的结合清楚地表明，来自两种转化体的大T蛋白至少表现出，至少用于该特定的生物化学功能，相同的体外温度敏感性。在一种类型的转化体中，只能在限制温度生长的细胞的提取物中检测到减少的结合活性。因此，可以通过与细胞组分的相互作用的新合成的大型T蛋白的体内稳定化来导致转化体的温度无关行为。

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