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
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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.
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