RNA肿瘤病毒逆转录酶的研究。I. 热不稳定DNA聚合酶和核糖核酸酶H活性在一条多肽链上的定位。
Studies on reverse transcriptase of RNA tumor viruses. I. Localization of thermolabile DNA polymerase and RNase H activities on one polypeptide.
作者信息
Verma I M
出版信息
J Virol. 1975 Jan;15(1):121-6. doi: 10.1128/JVI.15.1.121-126.1975.
Abstract
Purified reverse transcriptase from avian myeloblastosis virus or Rous sarcoma virus consists of two subunits of average mol wt of 100,000 and 60,000. The lower-molecular-weight subunit, alpha, has been isolated from avian myeloblastosis virus, Rous sarcoma virus and a temperature-sensitive mutant of Rous sarcoma virus, LA337. Subunit alpha manifests both the DNA polymerase and RNase H activities associated with purified reverse transcriptase of avian RNA tumor viruses. The thermal inactivation of these enzymatic activities of alpha subunit from the wild-type virus. The results show that both DNA polymerase and RNase H activities associated with the alpha subunit of LA337 are five to seven times more thermolabile then the corresponding alpha subunit from the wild-type virus. It is concluded that (i) both the polymerase and nuclease activities reside on the same polypeptide chain, and (ii) at least the lower-molecular-weight subunit alpha is coded for by the viral RNA.
摘要
来自禽成髓细胞瘤病毒或劳氏肉瘤病毒的纯化逆转录酶由两个亚基组成，平均分子量分别为100,000和60,000。分子量较低的亚基α已从禽成髓细胞瘤病毒、劳氏肉瘤病毒以及劳氏肉瘤病毒的温度敏感突变体LA337中分离出来。亚基α表现出与禽RNA肿瘤病毒纯化逆转录酶相关的DNA聚合酶和核糖核酸酶H活性。野生型病毒α亚基的这些酶活性的热失活。结果表明，与LA337的α亚基相关的DNA聚合酶和核糖核酸酶H活性的热稳定性比野生型病毒相应的α亚基低五到七倍。得出的结论是：(i) 聚合酶和核酸酶活性都存在于同一条多肽链上，(ii) 至少分子量较低的亚基α是由病毒RNA编码的。
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