Zhou Q, Boyer T G, Berk A J
Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024-1570.
Genes Dev. 1993 Feb;7(2):180-7. doi: 10.1101/gad.7.2.180.
TFIID is a multisubunit protein containing the TATA box-binding polypeptide (TBP) and associated factors (TFIID-TAFs) required for activated transcription by RNA polymerase II. TBPs from different eukaryotes contain a highly conserved carboxy-terminal domain and very divergent amino-terminal domains. Earlier studies proposed that the amino-terminal domains of metazoan TBPs are required for activated transcription. However, we report that a human TFIID complex containing an amino-terminal truncated TBP contains all the major TFIID-TAFs and supports in vitro transcriptional stimulation by different classes of activation domains and from a TATA-less promoter. Protein blotting experiments revealed direct interactions between the conserved domain of TBP and the two largest TAFs. The results suggest a model for the interaction of TFIID-TAFs with TBP.
TFIID是一种多亚基蛋白，包含TATA框结合多肽（TBP）和RNA聚合酶II激活转录所需的相关因子（TFIID-TAFs）。来自不同真核生物的TBP含有高度保守的羧基末端结构域和差异很大的氨基末端结构域。早期研究表明，后生动物TBP的氨基末端结构域是激活转录所必需的。然而，我们报道，含有氨基末端截短TBP的人TFIID复合物包含所有主要的TFIID-TAFs，并支持不同类型激活结构域以及来自无TATA框启动子的体外转录刺激。蛋白质印迹实验揭示了TBP保守结构域与两个最大TAFs之间的直接相互作用。结果提示了一个TFIID-TAFs与TBP相互作用的模型。
