A transformation-defective mutant of Abelson murine leukemia virus lacks protein kinase activity.
A transformation-defective mutant of Abelson murine leukemia virus lacks protein kinase activity.
复制标题
阿贝尔森鼠白血病病毒的转化缺陷突变体缺乏蛋白激酶活性。
DOI：
10.1073/pnas.77.8.4993
复制
发表时间：
1980
影响因子：
11.1
通讯作者：
Baltimore,D
中科院分区：
文献类型：
--
作者：
Witte,ON;Goff,S;Rosenberg,N;Baltimore,D
Abelson鼠白血病病毒（A-MuLV）的一个转化缺陷突变体，称为A-MuLV-P92 td。该突变体编码分子量为92，000（P92）的血清学可识别A-MuLV蛋白，但缺乏转化成纤维细胞或骨髓淋巴样细胞的能力。与通过转化A-MuLV菌株制备的蛋白质相反，通过A-MuLV-P92 td制备的蛋白质在与[γ-32 P]ATP体外孵育期间不被磷酸化。如果蛋白质与来自由功能性A-MuLV株转化的细胞的蛋白质混合，则发生P92的磷酸化，表明其接受磷酸盐的能力不会因突变而改变。这些平行变化提供了遗传证据，证明A-MuLV蛋白是一种转化蛋白，其相关的蛋白激酶活性（EC 2.7.1.37）是其转化能力的关键部分。
A transformation-defective mutant of Abelson murine leukemia virus (A-MuLV), called A-MuLV-P92td, has been isolated. The mutant encodes a serologically identifiable A-MuLV protein of molecular weight 92,000 (P92) but it lacks the ability to transform either fibroblasts or bone marrow lymphoid cells. In contrast to the protein made by transforming strains of A-MuLV, the protein made by A-MuLV-P92td does not becme phosphorylated during in vitro incubation with [gamma-32P]ATP. If the protein is mixed with proteins from cells transformed by a functional A-MuLV strain, phosphorylation of P92 occurs, showing that its ability to accept phosphate is not altered by the mutation. These parallel changes provide genetic evidence that the A-MuLV protein is a transforming protein and that its associated protein kinase activity (EC 2.7.1.37) is a crucial part of its transforming ability.