AFFINITY PURIFICATION OF TRANSCRIPTION FACTOR-IIA FROM HELA-CELL NUCLEAR EXTRACTS

被引：38

作者：

USUDA, Y

KUBOTA, A

BERK, AJ

HANDA, H

机构：

[1] UNIV CALIF LOS ANGELES,INST MOLEC BIOL,LOS ANGELES,CA 90024

[2] UNIV CALIF LOS ANGELES,DEPT MICROBIOL,LOS ANGELES,CA 90024

来源：

EMBO JOURNAL | 1991年 / 10卷 / 08期

关键词：

AFFINITY PURIFICATION; HUMAN TFIIA; PROTEIN INTERACTION; TRANSCRIPTION; YEAST TFIID;

D O I：

10.1002/j.1460-2075.1991.tb07767.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2305 / 2310

页数：6

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