Abstract
ACTIVATOR proteins that control transcription initiation by RNA polymerase II1,2 usually have two domains: one binds to DNA, and the other activates transcription3,4. A particularly potent acidic5,6 activation domain at the C terminus of the herpes simplex virus protein VP167–9 binds directly and selectively to the human and yeast TAT A box-binding factor TFIID10. We have now investigated the biological significance of this in vitro interaction by using mutant forms of VP1611. For changes at the critical phenyl-alanine residue at position 442 of VP16 there was a good correla-tion between transactivation activity in vivo and the binding of VP16 to TFIID in vitro. In contrast, mutants with reduced negative charge were more defective for binding than for activation.
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Ingles, C., Shales, M., Cress, W. et al. Reduced binding of TFIID to transcriptionally compromised mutants of VP16. Nature 351, 588–590 (1991). https://doi.org/10.1038/351588a0
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DOI: https://doi.org/10.1038/351588a0
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