摘要
酵母转录激活因子GCN4调控细胞中氨基酸的生物合成,是典型的含bZIP结构域的DNA结合蛋白.本文合成了天然蛋白GCN4的碱性区(226-252),并在其N末端引入色氨酸残基W,做为单体肽GCN4-W.圆二色(CD)实验表明,突变后的单体肽仍能序列特异性识别DNA结合位点AP-1和ATF/CREB.用荧光滴定方法获得了GCN4-W与DNA位点结合形成复合物的表观解离常数.
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.
出处
《物理化学学报》
SCIE
CAS
CSCD
北大核心
2003年第9期834-838,共5页
Acta Physico-Chimica Sinica
基金
国家自然科学基金(20173001
2020331)~~
