Induced α Helix in the VP16 Activation Domain upon Binding to a Human TAF

@article{Uesugi1997InducedH,
  title={Induced $\alpha$ Helix in the VP16 Activation Domain upon Binding to a Human TAF},
  author={Motonari Uesugi and Orig{\`e}ne Nyanguile and Hua Lu and Arnold J. Levine and Gregory L. Verdine},
  journal={Science},
  year={1997},
  volume={277},
  pages={1310-1313}
}
Activation domains are functional modules that enable sequence-specific DNA binding proteins to stimulate transcription. The structural basis for the function of activation domains is poorly understood. A combination of nuclear magnetic resonance (NMR) and biochemical experiments revealed that the minimal acidic activation domain of the herpes simplex virus VP16 protein undergoes an induced transition from random coil to α helix upon binding to its target protein, hTAFII31 (a human TFIID TATA… Expand
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The mechanism of transcriptional activation by VP16 and other proteins may involve both ionic and specific hydrophobic interactions with target molecules. Expand
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The design of an artificial protein bearing a novel 15-amino acid peptide linked to a DNA binding fragment of the yeast regulatory protein GAL4 is reported, which efficiently activates the GAL1 gene which is ordinarily activated by GAL 4. Expand
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  • Proceedings of the National Academy of Sciences of the United States of America
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TLDR
Results demonstrate that TAFII31 is a coactivator for the p53 protein, a critical protein required for p53-mediated transcriptional activation. Expand
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TLDR
Two conclusions are led: first, the acidic amino acids are not, as commonly thought, required for activation; second, this region is not unstructured or alpha helical, but its function may require a beta sheet. Expand
Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIB
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TLDR
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TLDR
The overproduced and purified carboxy-terminal transactivation domain of Vmw65 (VP16) of herpes simplex virus and potential folding of the domain by 1H NMR indicate that the isolated acid domain has little if any alpha-helical content of any stable nature. Expand
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TLDR
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Structural features of the transcriptional activation domain of the herpes simplex virion protein VP16 were examined by oligonucleotide-directed mutagenesis. Extensive mutagenesis at position 442 ofExpand
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