Zhao Dongxin, Huang Zhongxian
School of Chemistry and Chemical Engineering, Henan University of Technology, Zhengzhou 450001, China.
Department of Chemistry, Fudan University, Shanghai 200433, China.
Bioinorg Chem Appl. 2015;2015:416751. doi: 10.1155/2015/416751. Epub 2015 Sep 20.
ZNF191(243-368) is the C-terminal region of ZNF191 which contains a putative DNA-binding domain of four Cys2His2 zinc finger motifs. In this study, an expression vector of a fusion protein of ZNF191(243-368) with glutathione-S-transferase (GST) was constructed and transformed into Escherichia coli BL21. The fusion protein GST-ZNF191(243-368) was expressed using this vector to investigate the protein-DNA binding reaction through an affinity selection strategy on the basis of the binding quality of the zinc finger domain. Results showed that ZNF191(243-368) can selectively bind with sequences and react with genes which contain an AGGG core. However, the recognition mechanism of Cys2His2 zinc finger proteins to DNA warrants further investigation.
ZNF191(243 - 368)是ZNF191的C末端区域，它包含一个由四个Cys2His2锌指基序组成的假定DNA结合结构域。在本研究中，构建了ZNF191(243 - 368)与谷胱甘肽 - S - 转移酶(GST)的融合蛋白表达载体，并将其转化到大肠杆菌BL21中。利用该载体表达融合蛋白GST - ZNF191(243 - 368)，基于锌指结构域的结合特性，通过亲和选择策略研究蛋白与DNA的结合反应。结果表明，ZNF191(243 - 368)能够与含有AGGG核心的序列选择性结合并与基因发生反应。然而，Cys2His2锌指蛋白对DNA的识别机制仍有待进一步研究。
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