Perkins N D, Nicolas R H, Plumb M A, Goodwin G H
Institute of Cancer Research, Chester Beatty Laboratories, London, UK.
Nucleic Acids Res. 1989 Feb 25;17(4):1299-314. doi: 10.1093/nar/17.4.1299.
An erythroid nuclear protein (EF1), originally detected as a protein binding within the nuclease hypersensitive site upstream of the chicken beta H-globin gene, has been purified. This protein of 37,000-39,000 molecular weight binds to three sites within the hypersensitive region: one between the CCAAT and TATA boxes, the second (further upstream) next to a NF1 binding site, and the third adjacent to a regulatory element found in a number of beta-globin genes. The EF1 protein also binds to an erythroid-specific promoter element of the mouse alpha-globin gene and to two sites within the chicken beta A-globin enhancer. These six EF1-binding sites are related by the consensus sequence A/TGATAA/GG/C. A minor protein of molecular weight 72,000 which co-purifies with EF1 also binds to the same sequences.
一种红系核蛋白(EF1)已被纯化,最初它被检测为一种能与鸡β-H珠蛋白基因上游核酸酶超敏位点内的序列结合的蛋白质。这种分子量为37,000 - 39,000的蛋白质与超敏区域内的三个位点结合:一个在CCAAT盒和TATA盒之间,第二个(更上游)紧邻一个NF1结合位点,第三个与许多β-珠蛋白基因中发现的一个调控元件相邻。EF1蛋白还与小鼠α-珠蛋白基因的一个红系特异性启动子元件以及鸡β-A珠蛋白增强子内的两个位点结合。这六个EF1结合位点通过共有序列A/TGATAA/GG/C相关联。一种分子量为72,000且与EF1共纯化的次要蛋白质也与相同序列结合。