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首页> 外文期刊>Molecular and Cellular Biology >Analysis of functional domains of the v-fms-encoded protein of Susan McDonough strain feline sarcoma virus by linker insertion mutagenesis.
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Analysis of functional domains of the v-fms-encoded protein of Susan McDonough strain feline sarcoma virus by linker insertion mutagenesis.

机译：Susan McDonough应变猫肉瘤病毒的v-fms编码蛋白的功能域通过接头插入诱变分析。

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摘要

The Susan McDonough strain of feline sarcoma virus contains an oncogene, v-fms, which is capable of transforming fibroblasts in vitro. The mature protein product of the v-fms gene (gp140fms) is found on the surface of transformed cells; this glycoprotein has external, transmembrane, and cytoplasmic domains. To assess the functional role of these domains in transformation, we constructed a series of nine linker insertion mutations throughout the v-fms gene by using a dodecameric BamHI linker. The biological effects of these mutations on the function and intracellular localization of v-fms-encoded proteins were determined by transfecting the mutated DNA into Rat-2 cells. Most of the mutations within the external domain of the v-fms-encoded protein eliminated focus formation on Rat-2 cells; three of these mutations interfered with the glycosylation of the v-fms protein and interfered with formation of the mature gp140fms. One mutation in the external domain led to cell surface expression of v-fms protein even in the absence of complete glycosylational processing. Cell surface expression of mutated v-fms protein is probably necessary, but is not sufficient, for cell transformation since mutant v-fms protein was found on the surface of several nontransformed cell lines. Mutations that were introduced within the external domain had little effect on in vitro kinase activity, whereas mutations within the cytoplasmic domain all had strong inhibitory effects on this activity.
机译：Susan McDonough猫肉瘤病毒株含有一个癌基因v-fms，它能够在体外转化成纤维细胞。在转化细胞的表面发现了v-fms基因的成熟蛋白质产物（gp140fms）。该糖蛋白具有外部，跨膜和胞质结构域。为了评估这些域在转化中的功能作用，我们通过使用十二聚体BamHI接头在整个v-fms基因中构建了一系列九个接头插入突变。通过将突变的DNA转染到Rat-2细胞中，可以确定这些突变对v-fms编码蛋白的功能和细胞内定位的生物学影响。 v-fms编码的蛋白质外部结构域内的大多数突变消除了Rat-2细胞上的焦点形成。这些突变中的三个干扰v-fms蛋白的糖基化并干扰成熟gp140fms的形成。即使没有完整的糖基化过程，外部结构域中的一种突变也导致v-fms蛋白的细胞表面表达。突变的v-fms蛋白的细胞表面表达对于细胞转化可能是必要的，但还不够，因为在一些未转化的细胞系的表面发现了突变的v-fms蛋白。在外部结构域内引入的突变对体外激酶活性影响很小，而在细胞质结构域内的突变均对该活性具有很强的抑制作用。

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