Abstract
A CENTRAL issue in eukaryotic transcriptional regulation is the mechanism by which promoter-specific transcription factors (activators) stimulate transcription. Two lines of evidence indicate that the general transcription factor TFIIB is a pivotal component in the mechanism by which an acidic activator functions. First, during assembly of the preinitiation complex TFIIB binding is a rate-limiting step enhanced by an acidic activator1. Second, the TFIIB activity in a HeLa cell nuclear extract is specifically retained on a column containing an acidic activating region1. But because our previous study monitored only TFIIB activity, it remains possible that the interaction between TFIIB and the acidic activating region is mediated through additional proteins, for example, those designated as adaptors2, coactivators3 or mediators4,5. A complementary clone encoding TFIIB has recently been isolated and shown to encode a polypeptide of relative molecular mass 35,000 (ref. 6). Here we report that TFIIB expressed in and purified from Escherichia coli (recombinant TFIIB) binds directly to the potent acidic activating region of the herpes simplex virus-1 VP16 protein.
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Lin, YS., Ha, I., Maldonado, E. et al. Binding of general transcription factor TFIIB to an acidic activating region. Nature 353, 569–571 (1991). https://doi.org/10.1038/353569a0
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DOI: https://doi.org/10.1038/353569a0
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