Hutton F G, Turnell A S, Gallimore P H, Grand R J
CRC Institute for Cancer Studies, University of Birmingham, Edgbaston, UK.
Oncogene. 2000 Jan 20;19(3):452-62. doi: 10.1038/sj.onc.1203316.
The adenovirus early region 1B (Ad E1B) genes have no transforming capability of their own but markedly increase the transformation frequency of Ad E1A following co-transfection into mammalian cells. The larger E1B proteins of both Ad2/5 and Ad12 bind to p53 and inhibit its ability to transcriptionally activate other genes. We have previously demonstrated that synthetic peptides identical to the binding sites for p53 on both the Ad2 and Ad12 E1B proteins will disrupt the interaction in vivo and in vitro. In the work presented here we have examined the effects of complex dissociation on Ad E1-transformed human cells. It has been shown, using confocal microscopy, that when the peptide identical to the p53 binding site was added to Ad5 E1-transformed cells it initally located in the cytoplasmic dense bodies where it caused disruption of the p53/E1B complex. Peptide and p53 then translocated to the nucleus. In Ad12 E1-transformed cells the peptide localized in the nucleus directly and there caused a reorganization of p53 staining from a highly organized, 'flecked' distribution to one in which nuclear staining was homogeneous and diffuse. Peptides added to either Ad5 E1 or Ad12 E1 transformed cells resulted in the release of transcriptionally active p53. Interestingly, the level of p53 then fell presumably as a result of proteasomal action - this was probably a reflection of the short half-life of 'free' (i.e. dissociated) p53 compared to that of the bound protein. Free p53 did not cause apoptosis in target cells probably due to the presence of the smaller (19K) E1B proteins. However, addition of peptide leads to a significant reduction in cell growth rate. We have further demonstrated that a significant proportion of those cells which had taken up peptide had ceased DNA synthesis, probably due to a p53-induced cell cycle arrest. The role of the larger EIB protein during transformation is considered in view of these data.
腺病毒早期区域1B(Ad E1B)基因自身没有转化能力,但在共转染到哺乳动物细胞后能显著提高Ad E1A的转化频率。Ad2/5和Ad12的较大E1B蛋白都能与p53结合,并抑制其转录激活其他基因的能力。我们之前已经证明,与Ad2和Ad12 E1B蛋白上p53结合位点相同的合成肽会在体内和体外破坏这种相互作用。在本文介绍的工作中,我们研究了复合物解离对Ad E1转化的人细胞的影响。使用共聚焦显微镜已经表明,当将与p53结合位点相同的肽添加到Ad5 E1转化的细胞中时,它最初位于细胞质致密体中,在那里它导致p53/E1B复合物的破坏。然后肽和p53转移到细胞核中。在Ad12 E1转化的细胞中,肽直接定位在细胞核中,并在那里导致p53染色从高度有序的“斑点状”分布重新组织为核染色均匀且弥散的分布。添加到Ad5 E1或Ad12 E1转化细胞中的肽都会导致转录活性p53的释放。有趣的是,随后p53水平下降,推测是蛋白酶体作用的结果——这可能反映了“游离”(即解离)p53与结合蛋白相比半衰期较短。游离p53可能由于较小的(19K)E1B蛋白的存在而不会在靶细胞中引起凋亡。然而,添加肽会导致细胞生长速率显著降低。我们进一步证明,摄取肽的细胞中有很大一部分已经停止了DNA合成,这可能是由于p53诱导的细胞周期停滞。鉴于这些数据,考虑了较大EIB蛋白在转化过程中的作用。