Leng P, Brown D, Deb S, Deb S
UNIV TEXAS,HLTH SCI CTR,DEPT MICROBIOL,SAN ANTONIO,TX 78284.
Int J Oncol. 1995 Jan;6(1):251-9.
Human oncoprotein MDM2 inhibits p53-induced transcriptional activation of promoters containing p53-binding sites. In this report we show that MDM2 interacts with the human TATA binding protein (TBP), in vivo and in. vitro, in the absence of p53. The C-terminal boundary of the TBP-binding domain on MDM2 resides between amino acids 221 and 276, whereas the N-terminal boundary is beyond amino acid 120. Thus, the acidic domain of MDM2 overlaps with the TBP binding domain and is needed for the interaction. The C-terminal conserved domain of TBP is required for MDM2 binding. MDM2-TBP interaction suggests a p53-independent, transcription regulatory role of MDM2.
人类癌蛋白MDM2可抑制p53诱导的含p53结合位点启动子的转录激活。在本报告中，我们表明在体内和体外，在不存在p53的情况下MDM2可与人TATA结合蛋白（TBP）相互作用。MDM2上TBP结合域的C端边界位于氨基酸221和276之间，而N端边界在氨基酸120之外。因此，MDM2的酸性结构域与TBP结合域重叠，且该相互作用需要酸性结构域。TBP的C端保守结构域是MDM2结合所必需的。MDM2-TBP相互作用提示了MDM2具有不依赖p53的转录调节作用。
