Interaction between an acidic activator and transcription factor TFIIB is required for transcriptional activation.
How eukaryotic promoter-specific activator proteins (activators) stimulate transcription is a central question. We have previously shown that an acidic activator can directly interact with the general transcription factor TFIIB and increase its stable assembly into a preinitiation complex. We have proposed that this increase in TFIIB assembly is at least part of the mechanism by which an acidic activator functions. A prediction of this hypothesis is that a TFIIB mutant unable to interact with an acidic activator could not support activated transcription, and here we present experiments that verify this prediction. In conjunction with previous studies, our results argue that interaction between an acidic activator and TFIIB is necessary for transcriptional activation.
Roberts
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SG
Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605.
Ha
I
I
Maldonado
E
E
Reinberg
D
D
Green
M R
MR
D001665:Binding Sites; D003001:Cloning, Molecular; D005656:Fungal Proteins / Q000378:metabolism; D005982:Glutathione Transferase / Q000235:genetics; D006367:HeLa Cells; D017405:Herpes Simplex Virus Protein Vmw65 / Q000378:metabolism; D006801:Humans; D009154:Mutation; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D015534:Trans-Activators / Q000378:metabolism*; D035581:Transcription Factor TFIIB; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic
D005656:Fungal Proteins; C070633:Gal-VP16; D017405:Herpes Simplex Virus Protein Vmw65; D011993:Recombinant Fusion Proteins; D015534:Trans-Activators; D035581:Transcription Factor TFIIB; D014157:Transcription Factors; D005982:Glutathione Transferase