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首页> 外文期刊>Molecular and Cellular Biology >v-src mutations outside the carboxyl-coding region are not sufficient to fully activate transformation by pp60c-src in NIH 3T3 cells.
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v-src mutations outside the carboxyl-coding region are not sufficient to fully activate transformation by pp60c-src in NIH 3T3 cells.

机译：羧基编码区域外的v-src突变不足以完全激活NIH 3T3细胞中pp60c-src的转化。

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Previous studies have shown that carboxyl-terminal mutation of pp60c-src can activate its transforming ability. Conflicting results have been reported for the transforming ability of pp60c-src mutants having only mutations outside its carboxyl-terminal region. To clarify the effects of such mutations, we tested the activities of chimeric v(amino)- and c(carboxyl)-src (v/c-src) proteins at different dosages in NIH 3T3 cells. The focus-forming activity of Rous sarcoma virus long terminal repeat (LTR)-src expression plasmids was significantly reduced when the v-src 3' coding region was replaced with the corresponding c-src region. This difference was masked when the Rous sarcoma virus LTR was replaced with the Moloney murine leukemia virus LTR, which induced approximately 20-fold more protein expression, but even focus-selected lines expressing v/c-src proteins were unable to form large colonies in soft agarose or tumors in NFS mice. This suggests that pp60c-src is not equally sensitive to mutations in its different domains and that there are at least two distinguishable levels of regulation, the dominant one being associated with its carboxyl terminus. v/c-src chimeric proteins expressed with either LTR had high in vitro specific kinase activity equal to that of pp60v-src but, in contrast, were phosphorylated at both Tyr-527 and Tyr-416. Total cell protein phosphotyrosine was enhanced in cells incompletely transformed by v/c-src proteins to the same extent as in v-src-transformed cells, suggesting that the carboxyl-terminal region may affect substrate specificity in a manner that is important for transformation.
机译：先前的研究表明，pp60c-src的羧基末端突变可以激活其转化能力。已经报道了仅在其羧基末端区域之外具有突变的pp60c-src突变体的转化能力有矛盾的结果。为了阐明此类突变的影响，我们测试了NIH 3T3细胞中不同剂量的嵌合v（氨基）-和c（羧基）-src（v / c-src）蛋白的活性。当将v-src 3'编码区替换为相应的c-src区时，劳斯肉瘤病毒长末端重复序列（LTR）-src表达质粒的聚焦活性大大降低。当劳斯肉瘤病毒LTR替换为莫洛尼鼠白血病病毒LTR时，这种差异被掩盖了，后者诱导了大约20倍的蛋白质表达，但即使表达v / c-src蛋白质的焦点选择品系也无法在大肠杆菌中形成大菌落。 NFS小鼠中的软琼脂糖或肿瘤。这表明pp60c-src对不同结构域的突变并不同样敏感，并且存在至少两个可区分的调节水平，主要水平与其羧基末端相关。用任一LTR表达的v / c-src嵌合蛋白均具有与pp60v-src相同的高体外比激酶活性，但相比之下，它们在Tyr-527和Tyr-416处均被磷酸化。由v / c-src蛋白质不完全转化的细胞中的总细胞蛋白质磷酸酪氨酸增强程度与v-src转化的细胞中的程度相同，表明羧基末端区域可能以对转化重要的方式影响底物特异性。

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