Larminie C G, Sutcliffe J E, Tosh K, Winter A G, Felton-Edkins Z A, White R J
Institute of Biomedical and Life Sciences, Division of Biochemistry and Molecular Biology, University of Glasgow, Glasgow G12 8QQ, United Kingdom.
Mol Cell Biol. 1999 Jul;19(7):4927-34. doi: 10.1128/MCB.19.7.4927.
RNA polymerase (Pol) III transcription is abnormally active in fibroblasts that have been transformed by simian virus 40 (SV40). This report presents evidence that two separate components of the general Pol III transcription apparatus, TFIIIB and TFIIIC2, are deregulated following SV40 transformation. TFIIIC2 subunits are expressed at abnormally high levels in SV40-transformed cells, an effect which is observed at both protein and mRNA levels. In untransformed fibroblasts, TFIIIB is subject to repression through association with the retinoblastoma protein RB. The interaction between RB and TFIIIB is compromised following SV40 transformation. Furthermore, the large T antigen of SV40 is shown to relieve repression by RB. The E7 oncoprotein of human papillomavirus can also activate Pol III transcription, an effect that is dependent on its ability to bind to RB. The data provide evidence that both TFIIIB and TFIIIC2 are targets for activation by DNA tumor viruses.
RNA聚合酶(Pol)III转录在被猴病毒40(SV40)转化的成纤维细胞中异常活跃。本报告提供的证据表明,通用Pol III转录装置的两个独立组分,即TFIIIB和TFIIIC2,在SV40转化后失调。TFIIIC2亚基在SV40转化的细胞中以异常高水平表达,在蛋白质和mRNA水平均观察到这种效应。在未转化的成纤维细胞中,TFIIIB通过与视网膜母细胞瘤蛋白RB结合而受到抑制。SV40转化后,RB与TFIIIB之间的相互作用受损。此外,SV40的大T抗原可解除RB的抑制作用。人乳头瘤病毒的E7癌蛋白也可激活Pol III转录,这种效应取决于其与RB结合的能力。这些数据提供了证据,表明TFIIIB和TFIIIC2都是DNA肿瘤病毒激活的靶点。