Functional expression of DNA binding domain of Zif268 in Escherichia coli.
- Author:
Zhi-Hu ZHAO
1
;
Quan-Bin XU
;
Qing-Jun MA
Author Information
1. Beijing Institute of Biotechnology, Beijing 100850, China. zhaozh@nic.bmi.ac.cn
- Publication Type:Journal Article
- MeSH:
DNA-Binding Proteins;
genetics;
Electrophoretic Mobility Shift Assay;
Escherichia coli;
genetics;
metabolism;
Gene Expression;
Genetic Vectors;
genetics;
Zinc Fingers;
genetics
- From:
Chinese Journal of Biotechnology
2004;20(3):352-355
- CountryChina
- Language:Chinese
-
Abstract:
As the ubiquitous nucleic acids recognizing motif, Zinc finger protein play important role in regulation of gene expression. The study of recognization specific will greatly facilitate understanding the delicate interaction of Zinc finger protein and DNA. By the choice of expression vector, the induction and culture conditions, the DNA binding domain of Zif268 was expressed in Escherichia coli partly solubly. The gel mobility shift assay shows that purified DNA binding domain can bind its natural target sequence specifically, which indicates the DNA binding domain remains its DNA binding activity in Escherichia coli. The functional expression of DNA binding domain of Zif268 will greatly facilitate the development of in vivo genetic selection assay for the study of Zinc fingers-DNA interaction.
