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Citation: Wang Xu, Deng Wei, Cao Ao-Neng, Lai Lu-Hua. Molecular Recognition of GCN4 Monomeric Peptide Tryptophane Mutant with Its DNA Target Sites[J]. Acta Physico-Chimica Sinica, ;2003, 19(09): 834-838. doi: 10.3866/PKU.WHXB20030911 shu

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

1.
State Key Laboratory for Structural Studies of Stable and Unstable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing　100871

Received Date: 24 March 2003
Available Online: 15 September 2003

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.
- Transcriptional activator(GCN4);CD;Fluorescence titration; 　Dissociation constant
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