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Affinity purification of transcription factor IIA from HeLa cell nuclear extracts.
Author(s) -
Usuda Y.,
Kubota A.,
Berk A.J.,
Handa H.
Publication year - 1991
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1991.tb07767.x
Subject(s) - bacteriology , hela , university hospital , library science , biology , medicine , family medicine , genetics , cell , computer science , bacteria
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.