Delineation of two functional regions of transcription factor TFIIB.

@article{Barberis1993DelineationOT,
  title={Delineation of two functional regions of transcription factor TFIIB.},
  author={Alcide Barberis and Christoph W M{\"u}ller and Stephen C Harrison and Mark Ptashne},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1993},
  volume={90 12},
  pages={5628-32}
}
Human transcription factor TFIIB, a protein of 316 amino acids, was subjected to limited proteolysis in order to define stable structural domains. We find that the C-terminal region of TFIIB, residues 106-316, is relatively stable, while the N-terminal region is very sensitive to proteases. Like full-length TFIIB, the stable domain, which we refer to as TFIIBc, interacts with the TATA-binding protein (TBP) on DNA. However, TFIIBc is unable to substitute for TFIIB in an in vitro transcription… CONTINUE READING

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