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 Hilton Driscoll and E. Peter Geiduschek},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102},
  pages={15406 - 15411}
}
  • George A Kassavetis, Elisabetta Soragni, +1 author E. Peter Geiduschek
  • Published 2005
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 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

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    RNA Polymerase III Transcription

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