Related Experiment Video
Updated: Aug 12, 2026

The Multifaceted Benefits of Protein Co-expression in Escherichia coli
Published on: February 5, 2015
[Functional expression of DNA binding domain of Zif268 in Escherichia coli]
Zhi-Hu Zhao1, Quan-Bin Xu, Qing-Jun Ma
1Beijing Institute of Biotechnology, Beijing 100850, China. zhaozh@nic.bmi.ac.cn
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.
More Related Videos
Related Concept Videos
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Cooperative Binding of Transcription Regulators
Single-Strand DNA Binding Proteins
Restriction Enzymes
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...
Cooperative Binding of Transcription Regulators

