Separation of the Transcriptional Coactivator and Antirepression Functions of Transcription Factor IIA

Human transcription factor IIA (TFIIA) is composed of three subunits (α , β , and γ ). TFIIA interacts with the TATA-box binding protein and can overcome repression of transcription. TFIIA was found to be necessary for VP16-mediated transcriptional activation through a coactivator function. We have...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1996-06, Vol.93 (13), p.6583-6588
Hauptverfasser: Ma, Dongmin, Olave, Ivan, Merino, Alejandro, Reinberg, Danny
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Sprache:eng
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Zusammenfassung:Human transcription factor IIA (TFIIA) is composed of three subunits (α , β , and γ ). TFIIA interacts with the TATA-box binding protein and can overcome repression of transcription. TFIIA was found to be necessary for VP16-mediated transcriptional activation through a coactivator function. We have separated the coactivator and antirepression activities of TFIIA. A TFIIA lacking the α subunit was isolated from HeLa cells. This ``mini-TFIIA'' interacts with the TATA-box binding protein and can overcome repression of transcription, but it is defective in transcriptional coactivator function.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.93.13.6583