Molecular recognition of GCN4 monomeric peptide tryptophane mutant with its DNA target sites

作者：Wang X; Deng W; Cao AN; Lai LH^*

来源：Acta Physico - Chimica Sinica, 2003, 19(9): 834-838.

• transcriptional activator (GCN4)
• CD
• fluorescence titration
• dissociation constant

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 synthesised the basic region (226-252) of natural protein GCN4, and introduced a Trp residue at the N-terminal. CD experimental data show that the synthesised 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.

• 出版日期2003-9
• 单位北京大学