Anti-cooperative biphasic equilibrium binding of transcription factor upstream stimulatory factor to its cognate DNA monitored by protein fluorescence changes.

@article{Sha1995AnticooperativeBE,
  title={Anti-cooperative biphasic equilibrium binding of transcription factor upstream stimulatory factor to its cognate DNA monitored by protein fluorescence changes.},
  author={Ming Sha and Adrian R. Ferr{\'e}-D'Amar{\'e} and Stephen K. Burley and Dixie J Goss},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 33},
  pages={19325-9}
}
Upstream stimulatory factor USF is a human transcriptional activation factor, which uses a basic/helix-loop-helix/ leucin zipper (b/HLH/Z) motif to homodimerize and recognize specific sequences in the promoter region of both nuclear and viral genes transcribed by RNA polymerase II. Steady state fluorescence spectroscopy demonstrated that the basic/helix-loop-helix/leucin zipper domain of USF binds its DNA targets with high affinity and specificity, whereas removal of the leucine zipper yielding… CONTINUE READING