Kutoh E, Schwander J
Dept. Innere Medizin, Kantonsspital Basel, Switzerland.
Biochem Biophys Res Commun. 1993 Aug 16;194(3):1475-82. doi: 10.1006/bbrc.1993.1991.
We report that Sp1 from nuclear extracts of BRL-3A cells interacts with the consensus DNA sequence for the Egr-1 gene product in an overlapping manner. Purified Sp1 failed to bind to this sequence and with the addition of sub-saturating level of nuclear extracts, the binding activity appeared. In Drosophila cells (SL2), exogenously expressed Sp1 activated the transcription through the Egr-1 site. These findings suggest that Sp1 can be targeted to a non-Sp1 (Egr-1) site with a cellular factor(s) and can activate the transcription through this element.
我们报告称，来自BRL-3A细胞核提取物的Sp1以重叠方式与Egr-1基因产物的共有DNA序列相互作用。纯化的Sp1未能结合该序列，而添加亚饱和水平的核提取物后，结合活性出现。在果蝇细胞（SL2）中，外源表达的Sp1通过Egr-1位点激活转录。这些发现表明，Sp1可通过一种细胞因子靶向非Sp1（Egr-1）位点，并可通过该元件激活转录。
