Purification and Biochemical Characterization of the Promoter-Specific Transcription Factor, Sp1

作者：Michael R. Briggs, James T. Kadonaga, Stephen P. Bell, Robert Tjian · 发表于：Science · 年份：1986 · DOI：10.1126/science.3529394 · 被引用次数：1487 · 研究领域：Genomics and Chromatin Dynamics、RNA Interference and Gene Delivery、RNA Research and Splicing

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.