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v-jun编码一种具有AP-1增强子结合特性的核蛋白。

v-jun encodes a nuclear protein with enhancer binding properties of AP-1.

作者信息

Bos T J, Bohmann D, Tsuchie H, Tjian R, Vogt P K

机构信息

Department of Microbiology, University of Southern California, School of Medicine, Los Angeles 90033.

出版信息

Cell. 1988 Mar 11;52(5):705-12. doi: 10.1016/0092-8674(88)90408-4.

Abstract

The jun oncogene of ASV17 is expressed as a 65 kd protein (p65gag-jun) that contains partial gag sequences at its amino terminus fused to jun sequences that make up the carboxy terminal two-thirds of the molecule. As a first step toward evaluating potential functional differences between the activated oncogene, v-jun, and its cellular counterpart, c-jun, we have characterized the biochemical properties of the gag-jun product of ASV17. Immunofluorescence studies revealed that the v-jun protein is localized in the nucleus of CEF transfected with ASV17 DNA. DNAase I foot-printing analysis indicates that p65gag-jun synthesized in bacteria binds to enhancer elements in SV40 that are recognition sites for the human transcription factor AP-1. Analysis of point mutants confirmed that v-jun protein binds with DNA sequence specificity of the mammalian enhancer factor AP-1 and the yeast transcription factor GCN4. These findings suggest that activation of the jun oncogene may not exclusively be the result of alterations in the DNA binding properties of the normal cellular protein.

摘要

ASV17的jun癌基因表达为一种65kd的蛋白质(p65gag-jun),该蛋白质在其氨基末端含有部分gag序列,与构成分子羧基末端三分之二的jun序列融合。作为评估活化癌基因v-jun与其细胞对应物c-jun之间潜在功能差异的第一步,我们已经对ASV17的gag-jun产物的生化特性进行了表征。免疫荧光研究表明,v-jun蛋白定位于用ASV17 DNA转染的CEF细胞核中。DNA酶I足迹分析表明,在细菌中合成的p65gag-jun与SV40中的增强子元件结合,这些元件是人类转录因子AP-1的识别位点。点突变分析证实,v-jun蛋白与哺乳动物增强子因子AP-1和酵母转录因子GCN4的DNA序列特异性结合。这些发现表明,jun癌基因的激活可能并非仅仅是正常细胞蛋白DNA结合特性改变的结果。

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