Affinity purification of transcription factor IIA from HeLa cell nuclear extracts.
Affinity purification of transcription factor IIA from HeLa cell nuclear extracts.
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从 HeLa 细胞核提取物中亲和纯化转录因子 IIA。
DOI：
10.1002/j.1460-2075.1991.tb07767.x
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
H. Handa
中科院分区：
文献类型：
--
作者：
Y. Usuda;A. Kubota;A. J. Berk;H. Handa
通过酵母 TFIID 亲和层析，从 HeLa 细胞核提取物中纯化出一种通用转录因子 TFIIA。人 TFIIA 的分子量约为 38 kd。它能够与酵母 TFIID 和腺病毒 E4 和 ML 启动子以及 HSP70 启动子的 TATA 元件形成的复合物结合。该协会通过 DNase I 消化的酵母 TFIID 扩展了每个 TATA 元件上的受保护区域。亲和纯化的 TFIIA 还能够在体外重构系统中刺激 E4 和 ML 启动子的转录。
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.