Acta Phys. -Chim. Sin. ›› 2003, Vol. 19 ›› Issue (09): 834 -838.doi: 10.3866/PKU.WHXB20030911

• ARTICLE • Previous Articles     Next Articles

Molecular Recognition of GCN4 Monomeric Peptide Tryptophane Mutant with Its DNA Target Sites

Wang Xu;Deng Wei;Cao Ao-Neng;Lai Lu-Hua   

  1. State Key Laboratory for Structural Studies of Stable and Unstable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871
  • Received:2003-03-24 Revised:2003-05-06 Published:2003-09-15
  • Contact: Lai Lu-Hua E-mail:lhlai@pku.edu.cn

Abstract: The transcriptional activator GCN4 plays a key role in the regulation of amino acid anabolism in yeast. It is a DNA binding protein that has typical bZIP domain. We synthesized the basic region (226-252) of natural protein GCN4, and introduced a Trp residue at the N-terminal. CD experimental data show that the synthesized monomer peptide, GCN4-W, can still specifically recognize the DNA target sites AP-1 and ATF/CREB. We also obtained the apparent dissociation constant of the peptide-DNA complex of this monomer recognizing DNA site by fluorescence titration method.

Key words: Transcriptional activator(GCN4), CD, Fluorescence titration,  Dissociation constant