从HeLa细胞核提取物中亲和纯化转录因子IIA。

Usuda Y, Kubota A, Berk A J, Handa H

Department of Bacteriology, University of Tokyo Faculty of Medicine, Japan.

EMBO J. 1991 Aug;10(8):2305-10. doi: 10.1002/j.1460-2075.1991.tb07767.x.

One of the general transcription factors, TFIIA, was purified to homogeneity from HeLa cell nuclear extracts by yeast TFIID affinity chromatography. Human TFIIA had a molecular weight of approximately 38 kd. It was able to associate with the complex formed by yeast TFIID and the TATA elements of the adenovirus E4 and ML promoters, and the HSP70 promoter. The association extended the protected region on each TATA element by yeast TFIID from DNase I digestion. Affinity-purified TFIIA was also able to stimulate transcription from the E4 and ML promoters in in vitro reconstituted systems.

通用转录因子之一TFIIA，通过酵母TFIID亲和层析从HeLa细胞核提取物中纯化至同质。人TFIIA的分子量约为38kd。它能够与酵母TFIID与腺病毒E4和ML启动子以及HSP70启动子的TATA元件形成的复合物结合。这种结合扩展了酵母TFIID对每个TATA元件免受DNase I消化的保护区域。亲和纯化的TFIIA在体外重组系统中也能够刺激E4和ML启动子的转录。