SPECIES-SPECIFIC INTERACTION OF THE GLUTAMINE-RICH ACTIVATION DOMAINS OF SP1 WITH THE TATA BOX-BINDING PROTEIN
SPECIES-SPECIFIC INTERACTION OF THE GLUTAMINE-RICH ACTIVATION DOMAINS OF SP1 WITH THE TATA BOX-BINDING PROTEIN
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DOI：
10.1128/mcb.14.3.1582
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发表时间：
1994-03-01
影响因子：
5.3
通讯作者：
INGLES, CJ
中科院分区：
文献类型：
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作者：
EMILI, A;GREENBLATT, J;INGLES, CJ
我们使用蛋白质印迹和蛋白质亲和层析来证明人转录因子 Sp1 的两个富含谷氨酰胺的激活结构域中的每一个都可以特异性地直接结合到人 TATA 盒结合蛋白 (TBP) 的 C 端进化保守结构域。 Sp1 的这些激活结构域也直接与果蝇 TBP 结合，但与来自酿酒酵母的 TBP 结合强度要低得多。 Sp1 激活结构域与不同物种的 TBP 直接相互作用的能力与其激活来自同一物种的提取物中的转录的能力密切相关。我们还表明，果蝇蛋白触角足富含谷氨酰胺的转录激活区域以物种特异性方式直接与 TBP 结合，这反映了其在体内激活转录的能力。这些结果支持这样的观点：TBP 是富含谷氨酰胺的转录激活剂的直接且重要的靶标。
We have used protein-blotting and protein affinity chromatography to demonstrate that each of the two glutamine-rich activation domains of the human transcription factor Sp1 can bind specifically and directly to the C-terminal evolutionarily conserved domain of the human TATA box-binding protein (TBP). These activation domains of Sp1 also bind directly to Drosophila TBP but bind much less strongly to TBP from the yeast Saccharomyces cerevisiae. The abilities of the Sp1 activation domains to interact directly with the TBPs of various species correlate well with their abilities to activate transcription in extracts derived from the same species. We also show that a glutamine-rich transcriptional activating region of the Drosophila protein Antennapedia binds directly to TBP in a species-specific manner that reflects its ability to activate transcription in vivo. These results support the notion that TBP is a direct and important target of glutamine-rich transcriptional activators.