DNA-BINDING ACTIVITY IS ASSOCIATED WITH PURIFIED MYB PROTEINS FROM AMV AND E26 VIRUSES AND IS TEMPERATURE-SENSITIVE FOR E26 TS MUTANTS
DNA-BINDING ACTIVITY IS ASSOCIATED WITH PURIFIED MYB PROTEINS FROM AMV AND E26 VIRUSES AND IS TEMPERATURE-SENSITIVE FOR E26 TS MUTANTS
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DOI：
10.1016/0092-8674(85)90358-7
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发表时间：
1985-01-01
期刊：
影响因子：
64.5
通讯作者：
GRAF, T
中科院分区：
文献类型：
--
作者：
MOELLING, K;PFAFF, E;GRAF, T
间接免疫荧光显示，禽成髓细胞增生症病毒(AMV)的癌基因蛋白产物p48v-MYB和禽白血病病毒E26的癌基因蛋白产物p135gag-MYB-Ets主要定位于非生成性骨髓细胞克隆的细胞核中。用抗p19和抗MYB免疫球蛋白的单抗进行免疫亲和层析，纯化两种癌基因蛋白，并在细菌中表达，以产生抗体。纯化的蛋白质在体外与DNA结合。从E26病毒的几个突变体中提纯的p135gag-MYB-ETS蛋白对骨髓细胞转化是温度敏感的，在体外要么失去与DNA结合的能力，要么表现出高度不耐热的DNA-蛋白质相互作用。AMV和E26癌基因蛋白的DNA结合被MYB特异性Ig抑制。这些结果表明，MYB癌基因的损伤在体外影响MYB蛋白的转化和DNA结合。
Oncogene protein products from avian myeloblastosis virus (AMV), p48v-myb, and from avian leukemia virus E26, p135gag-myb-ets, are located predominantly in the nucleus of nonproducer bone marrow cell clones, as revealed by indirect immunofluorescence. Both oncogene proteins were purified by immunoaffinity chromatography using monoclonal antibodies against p19 and Ig specific for myb, which was expressed in bacteria for antibody production. The purified proteins bind to DNA in vitro. Purified p135gag-myb-ets proteins from several mutants of E26 virus, temperature-sensitive for myeloblast transformation, either lost their abilities to bind to DNA or exhibited highly thermolabile DNA-protein interactions in vitro. DNA binding of AMV and E26 oncogene proteins is inhibited by myb-specific Ig. These results suggest that lesions in the myb oncogene affect transformation and DNA binding of myb proteins in vitro.