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首页> 外文期刊>Molecular and Cellular Biology >H-ras mutants lacking the epitope for the neutralizing monoclonal antibody Y13-259 show decreased biological activity and are deficient in GTPase-activating protein interaction.
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H-ras mutants lacking the epitope for the neutralizing monoclonal antibody Y13-259 show decreased biological activity and are deficient in GTPase-activating protein interaction.

机译：缺少中和性单克隆抗体Y13-259的表位的H-ras突变体显示出降低的生物活性，并且在GTPase激活蛋白相互作用中不足。

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摘要

We have generated deletion mutants of the H-ras p21 protein which lack residues 58 to 63 or 64 to 68 and contain either the normal glycine or an activating mutation, arginine, at position 12. None of the deleted proteins were recognized by monoclonal antibody Y13-259, and those mutants with activating mutations showed at least a 100-fold reduction in their transforming activities compared with the activities of their nondeleted counterparts. Alterations observed in the in vitro GTPase or GTP interchange properties of the deletion mutants were not consistent with the decrease in their transforming activities. Moreover, each mutant showed normal membrane localization, which is essential for its biological activity. Recently, a newly identified protein, designated GTPase-activating protein (GAP), was found to markedly increase GTPase activity of the normal ras p21 but not of p21 mutants bearing activating lesions (H. Adari, D. R. Lowy, B. M. Willumsen, C. J. Der, and F. McCormick, Science 240:518-521, 1988). We showed that GAP had no effect on the in vitro GTPase activity of the deletion mutants of the normal p21 protein. Since similar deletions in mutants with activating lesions at position 12 or 59 or both showed decreased transforming activity, our results suggest that the recognition site for Y13-259 within the ras p21 molecule influences directly or indirectly the interaction of ras p21 with GAP and that this interaction is critical for biological activity of ras proteins.
机译：我们已经生成了H-ras p21蛋白的缺失突变体，该突变体缺少58至63或64至68位残基，并在位置12处含有正常甘氨酸或活化突变精氨酸。所有缺失的蛋白均未被单克隆抗体Y13识别-259，并且那些具有激活突变的突变体与未删除的对应物相比，其转化活性降低了至少100倍。在缺失突变体的体外GTPase或GTP互换特性中观察到的变化与其转化活性的降低不一致。此外，每个突变体均显示正常的膜定位，这对其生物学活性至关重要。最近，发现了一种新鉴定的蛋白，称为GTPase激活蛋白（GAP），可显着增加正常ras p21的GTPase活性，但不能显着提高带有激活性病变的p21突变体的GTPase活性（H. Adari，DR Lowy，BM Willumsen，CJ Der， F.McCormick，科学240：518-521，1988）。我们表明，GAP对正常p21蛋白缺失突变体的体外GTPase活性没有影响。由于在具有第12或59位活化损伤的突变体中相似的缺失或两者均显示出降低的转化活性，因此我们的结果表明ras p21分子内Y13-259的识别位点直接或间接影响ras p21与GAP的相互作用，并且这相互作用对于ras蛋白的生物学活性至关重要。

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