Hoey T, Weinzierl R O, Gill G, Chen J L, Dynlacht B D, Tjian R
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Cell. 1993 Jan 29;72(2):247-60. doi: 10.1016/0092-8674(93)90664-c.
The general transcription factor TFIID is a multiprotein complex containing the TATA-binding protein and several associated factors (TAFs), some of which may function as coactivators that are essential for activated, but not basal, transcription. Here we describe the isolation and characterization of the first gene encoding a TAF protein. The deduced amino acid sequence of TAF110 revealed the presence of several glutamine- and serine/threonine-rich regions reminiscent of the protein-protein interaction domains of the regulatory transcription factor Sp1 that are involved in transcription activation and multimerization. In both Drosophila cells and yeast, TAF110 specifically interacts with the glutamine-rich activation domains of Sp1. Moreover, purified Sp1 selectively binds recombinant TAF110 in vitro. These findings taken together suggest that TAF110 may function as a coactivator by serving as a site of protein-protein contact between activators like Sp1 and the TFIID complex.
通用转录因子TFIID是一种多蛋白复合物，包含TATA结合蛋白和几种相关因子（TAF），其中一些可能作为共激活因子发挥作用，这些共激活因子对于激活转录而非基础转录至关重要。在此，我们描述了首个编码TAF蛋白的基因的分离和鉴定。TAF110推导的氨基酸序列显示存在几个富含谷氨酰胺和丝氨酸/苏氨酸的区域，这让人联想到参与转录激活和多聚化的调节转录因子Sp1的蛋白质-蛋白质相互作用结构域。在果蝇细胞和酵母中，TAF110都特异性地与Sp1富含谷氨酰胺的激活结构域相互作用。此外，纯化的Sp1在体外选择性结合重组TAF110。综合这些发现表明，TAF110可能通过充当Sp1等激活因子与TFIID复合物之间蛋白质-蛋白质接触的位点来发挥共激活因子的作用。
