Reconfiguring the connectivity of a multiprotein complex: fusions of yeast TATA-binding protein with Brf1, and the function of transcription factor IIIB.

@article{Kassavetis2005ReconfiguringTC,
  title={Reconfiguring the connectivity of a multiprotein complex: fusions of yeast TATA-binding protein with Brf1, and the function of transcription factor IIIB.},
  author={George A. Kassavetis and Elisabetta Soragni and Robert Driscoll and E. Peter Geiduschek},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 43},
  pages={15406-11}
}
Transcription factor (TF) IIIB, the central transcription initiation factor of RNA polymerase III (pol III), is composed of three subunits, Bdp1, Brf1 and TATA-binding protein (TBP), all essential for normal function in vivo and in vitro. Brf1 is a modular protein: Its N-proximal half is related to TFIIB and binds similarly to the C-terminal stirrup of TBP; its C-proximal one-third provides most of the affinity for TBP by binding along the entire length of the convex surface and N-terminal… CONTINUE READING