BAP37和Prohibitin被SV40 T抗原抗体特异性识别

Alison J. Darmon , Parmjit S. Jat
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引用次数: 7

摘要

我们已经鉴定了两种细胞蛋白,它们被抗sv40 T抗原单克隆抗体特异性免疫沉淀。这种名为PAb419的抗体可以识别包含在T抗原区域内的一个表位,我们最近证明了这个表位是SV40 T抗原启动永生所必需的,但对于维持永生状态不是必需的。这两个蛋白鉴定为BAP37和Prohibitin。最近的研究结果表明,prohibition可能会增强视网膜母细胞瘤口袋蛋白家族(pRb, p107, p130)对E2F的转录失活。BAP37和Prohibitin可被另一种具有重叠表位的抗sv40 T抗原单克隆抗体PAb419和PAb210特异性识别,但不能被其他抗sv40 T抗原单克隆抗体识别,证明了相互作用的特异性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
BAP37 and Prohibitin Are Specifically Recognized by an SV40 T Antigen Antibody

We have identified two cellular proteins that are specifically immunoprecipitated by an anti-SV40 T antigen monoclonal antibody. This antibody, PAb419, recognizes an epitope contained within a region of T antigen which we have recently demonstrated is required for the initiation of immortalization by SV40 T antigen, but is not essential for maintenance of the immortal state. The two proteins were identified as BAP37 and Prohibitin. Recent results suggest Prohibitin may enhance the transcriptional inactivation of E2F by the retinoblastoma family of pocket proteins (pRb, p107, p130). BAP37 and Prohibitin are specifically recognized by PAb419 and PAb210, another anti-SV40 T antigen monoclonal antibody, which has an overlapping epitope, but not by other anti-SV40 T antigen monoclonal antibodies, demonstrating the specificity of the interaction.

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