一个上游激活序列调控小鼠磷酸甘油酸激酶-1（Pgk-1）启动子，并与多种核蛋白结合。
An upstream activator sequence regulates the murine Pgk-1 promoter and binds multiple nuclear proteins.
作者信息
Sutherland L C, St-Arnaud R, McBurney M W
机构信息
Department of Biology, University of Ottawa, Ontario, Canada.
出版信息
Gene Expr. 1995;4(4-5):265-79.
The murine Pgk-1 gene is driven by a strong promoter that is regulated by a 304 bp upstream activator sequence (UAS). The activity of the UAS is high in undifferentiated embryonal carcinoma cells but declines when these cells are induced to differentiate with retinoic acid. The effect of the UAS on promoter activity is particularly striking when the activity of the Pgk-1 promoter is assayed following its integration into the genome, suggesting that it may function by regulating chromatin structure in the region of the core promoter. Three sites on the UAS bind nuclear proteins. Two of these sites bind factors present in both embryonal carcinoma cells and their differentiated derivatives whereas one site binds factors present only in differentiated cells. There appears to be both cooperation and antagonism in the binding of proteins to different sites in the UAS, suggesting that the activity of the Pgk-1 promoter is determined by the constellation of proteins assembled upstream of its transcription start site.
小鼠磷酸甘油酸激酶-1（Pgk-1）基因由一个强启动子驱动，该启动子受一个304 bp的上游激活序列（UAS）调控。UAS的活性在未分化的胚胎癌细胞中较高，但当这些细胞用视黄酸诱导分化时，其活性会下降。当将Pgk-1启动子整合到基因组中后检测其活性时，UAS对启动子活性的影响尤为显著，这表明它可能通过调节核心启动子区域的染色质结构来发挥作用。UAS上的三个位点结合核蛋白。其中两个位点结合胚胎癌细胞及其分化衍生物中都存在的因子，而一个位点只结合分化细胞中存在的因子。在蛋白质与UAS上不同位点的结合过程中似乎存在协同作用和拮抗作用，这表明Pgk-1启动子的活性是由其转录起始位点上游组装的蛋白质组合决定的。
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