Patch clamp and atomic force microscopy demonstrate TATA-binding protein (TBP) interactions with the nuclear pore complex

@article{Bustamante1995PatchCA,
  title={Patch clamp and atomic force microscopy demonstrate TATA-binding protein (TBP) interactions with the nuclear pore complex},
  author={Jos{\'e} Omar Bustamante and Andrejs Liepins and Robert A. Prendergast and John A Hanover and Hans Oberleithner},
  journal={The Journal of Membrane Biology},
  year={1995},
  volume={146},
  pages={263-272}
}
The universal TATA-binding protein, TBP, is an essential component of the multiprotein complex known as transcription factor IID (TFIID). This complex, which consists of TBP and TBP-associated factors (TAFs), is essential for RNA polymerase II-mediated transcription. The molecular size of human TBP (37.7 kD) is close to the passive diffusion limit along the transport channel of the nuclear pore complex (NPC). Therefore, the possibility exists that NPCs restrict TBP translocation to the nuclear… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 19 extracted citations

An historical perspective on cell mechanics

Pflügers Archiv - European Journal of Physiology • 2007

Glycan-dependent signaling: O-linked N-acetylglucosamine.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology • 2001

Similar Papers

Loading similar papers…