Molecular recognition: monomer of the yeast transcriptional activator GCN4 recognizes its dimer DNA binding target sites specifically

被引：0
|
作者：
曹炜
刘亮
来鲁华
唐有祺
机构：
[1] Beijing 100871
[2] Peking University
[3] Institute of Physical Chemistry
[4] China
[5] College of Chemistry and Molecular Engineering
来源：
Science in China(Series B) | 2000年 / 05期
关键词：
molecular recognition; conformational change; thermodynanlic parameter; ITC; CD;
D O I：
暂无
中图分类号：
O631 [高分子物理和高分子物理化学];
学科分类号：
摘要：
It is widely believed that dimerization is a requirement for the yeast transcriptional activator GCN4 to recognize its specific DNA target sites. We used the basic region (226-252) of the yeast transcriptional activator GCN4, as both a monomeric peptide and a disulfide-linked dimer to investigate the interaction of the peptides with the DNA target sites AP-1 and CRE. CD and ITC experiments indicate that although the monomeric peptide GCN4-M has a weaker affinity with the DNA relative to the disulfide-linked dimer peptide GCN4-D, it recognizes AP-1 and CRE target sites specifically.
引用
收藏
页码：466 / 476
页数：11
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