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Bioinorganic Chemistry and Applications
Volume 2015, Article ID 416751, 7 pages
Research Article

Recognition Code of ZNF191(243-368) and Its Interaction with DNA

1School of Chemistry and Chemical Engineering, Henan University of Technology, Zhengzhou 450001, China
2Department of Chemistry, Fudan University, Shanghai 200433, China

Received 29 May 2015; Accepted 2 September 2015

Academic Editor: Claudio Pettinari

Copyright © 2015 Dongxin Zhao and Zhongxian Huang. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.