Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID.
The potent transactivation domain of the herpes simplex virion protein VP16 was used as a column ligand for affinity chromatography. VP16 binds strongly and highly selectively to the human and yeast TATA box-binding factors. Our results imply that the principal target for acidic activation domains is the TATA-box factor TFIID.
Stringer
K F
KF
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada.
Ingles
C J
CJ
Greenblatt
J
J
D002846:Chromatography, Affinity; D006367:HeLa Cells; D006561:Herpes Simplex; D006801:Humans; D010750:Phosphoproteins / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D012319:RNA Polymerase II / Q000378:metabolism; D012045:Regulatory Sequences, Nucleic Acid; D012441:Saccharomyces cerevisiae / Q000235:genetics; D015534:Trans-Activators / Q000378:metabolism* / Q000648:ultrastructure; D014157:Transcription Factors / Q000378:metabolism* / Q000648:ultrastructure
D010750:Phosphoproteins; D015534:Trans-Activators; D014157:Transcription Factors; D012319:RNA Polymerase II