Separation of the transcriptional coactivator and antirepression functions of transcription factor IIA.
Human transcription factor IIA (TFIIA) is composed of three subunits (alpha, beta, and gamma). 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 alpha 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.
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Howard Hughes Medical Institute, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, 08854-5635, USA.
Olave
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Merino
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Reinberg
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D004268:DNA-Binding Proteins / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D012097:Repressor Proteins / Q000378:metabolism*; D016385:TATA Box; D035181:TATA-Box Binding Protein; D015534:Trans-Activators / Q000378:metabolism*; D035561:Transcription Factor TFIIA; D014157:Transcription Factors / Q000302:isolation & purification / Q000378:metabolism*; D014158:Transcription, Genetic
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C070633:Gal-VP16; D012097:Repressor Proteins; D035181:TATA-Box Binding Protein; D015534:Trans-Activators; D035561:Transcription Factor TFIIA; D014157:Transcription Factors