PURIFICATION AND BIOCHEMICAL-CHARACTERIZATION OF THE PROMOTER-SPECIFIC TRANSCRIPTION FACTOR, SPL
PURIFICATION AND BIOCHEMICAL-CHARACTERIZATION OF THE PROMOTER-SPECIFIC TRANSCRIPTION FACTOR, SPL
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DOI：
10.1126/science.3529394
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发表时间：
1986-10-03
期刊：
影响因子：
56.9
通讯作者：
TJIAN, R
中科院分区：
文献类型：
--
作者：
BRIGGS, MR;KADONAGA, JT;TJIAN, R
对参与启动子识别的细胞反式激活因子的生化分析为理解动物细胞中基因表达的机制提供了重要的一步。启动子选择性转录因子Sp1已通过序列特异性DNA亲和色谱法从人类细胞中纯化至95%以上的均一性。从十二烷基硫酸钠聚丙烯酰胺凝胶纯化的蛋白质的分离和复性允许识别的两个多肽（105和95千道尔顿）作为负责识别和相互作用的GC盒启动子元件特异性的Sp1结合位点。
The biochemical analysis of cellular trans-activators involved in promoter recognition provides an important step toward understanding the mechanisms of gene expression in animal cells. The promoter selective transcription factor, Sp1, has been purified from human cells to more than 95 percent homogeneity by sequence-specific DNA affinity chromatography. Isolation and renaturation of proteins purified from sodium dodecyl sulfate polyacrylamide gels allowed the identification of two polypeptides (105 and 95 kilodaltons) as those responsible for recognizing and interacting specifically with the GC-box promoter elements characteristic of Sp1 binding sites.