Zabierowski Susan E, Deluca Neal A
Biomedical Science Tower, Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA.
J Virol. 2008 Apr;82(7):3546-54. doi: 10.1128/JVI.02560-07. Epub 2008 Jan 23.
We have recently shown that ICP4 has a differential requirement for the general transcription factor TFIIA in vitro (S. Zabierowski and N. DeLuca, J. Virol. 78:6162-6170, 2004). TFIIA was dispensable for ICP4 activation of a late promoter (gC) but was required for the efficient activation of an early promoter (tk). An intact INR element was required for proficient ICP4 activation of the late promoter in the absence of TFIIA. Because TFIIA is known to stabilize the binding of both TATA binding protein (TBP) and TFIID to the TATA box of core promoters and ICP4 has been shown to interact with TFIID, we tested the ability of ICP4 to stabilize the binding of either TBP or TFIID to the TATA box of representative early, late, and INR-mutated late promoters (tk, gC, and gC8, respectively). Utilizing DNase I footprinting analysis, we found that ICP4 was able to facilitate TFIIA stabilized binding of TBP to the TATA box of the early tk promoter. Using mutant ICP4 proteins, the ability to stabilize the binding of TBP to both the wild-type and the INR-mutated gC promoters was located in the amino-terminal region of ICP4. When TFIID was substituted for TBP, ICP4 could stabilize the binding of TFIID to the TATA box of the wild-type gC promoter. ICP4, however, could not effectively stabilize TFIID binding to the TATA box of the INR-mutated late promoter. The additional activities of TFIIA were required to stabilize the binding of TFIID to the INR-mutated late promoter. Collectively, these data suggest that TFIIA may be dispensable for ICP4 activation of the wild-type late promoter because ICP4 can substitute for TFIIA's ability to stabilize the binding of TFIID to the TATA box. In the absence of a functional INR, ICP4 can no longer stabilize TFIID binding to the TATA box of the late promoter and requires the additional activities of TFIIA. The stabilized binding of TFIID by TFIIA may in turn allow ICP4 to more efficiently activate transcription from non-INR containing promoters.
我们最近发现,在体外,ICP4对通用转录因子TFIIA有不同的需求(S. Zabierowski和N. DeLuca,《病毒学杂志》78:6162 - 6170,2004年)。TFIIA对于ICP4激活晚期启动子(gC)是可有可无的,但对于有效激活早期启动子(tk)则是必需的。在没有TFIIA的情况下,完整的起始子元件(INR)对于晚期启动子的高效ICP4激活是必需的。因为已知TFIIA能稳定TATA结合蛋白(TBP)和TFIID与核心启动子TATA框的结合,并且已证明ICP4能与TFIID相互作用,所以我们测试了ICP4稳定TBP或TFIID与代表性早期、晚期及INR突变晚期启动子(分别为tk、gC和gC8)TATA框结合的能力。利用DNase I足迹分析,我们发现ICP4能够促进TFIIA稳定TBP与早期tk启动子TATA框的结合。使用突变的ICP4蛋白,稳定TBP与野生型和INR突变型gC启动子结合的能力位于ICP4的氨基末端区域。当用TFIID替代TBP时,ICP4能够稳定TFIID与野生型gC启动子TATA框的结合。然而,ICP4不能有效地稳定TFIID与INR突变晚期启动子TATA框的结合。需要TFIIA的额外活性来稳定TFIID与INR突变晚期启动子的结合。总体而言,这些数据表明,TFIIA对于野生型晚期启动子的ICP4激活可能是可有可无的,因为ICP4可以替代TFIIA稳定TFIID与TATA框结合的能力。在没有功能性INR的情况下,ICP不再能稳定TFIID与晚期启动子TATA框的结合,并且需要TFIIA的额外活性。TFIIA对TFIID结合的稳定反过来可能使ICP4更有效地激活不含INR的启动子的转录。