Construction and characterization of TetR and GFP fusion protein.
- Author:
Yan ZUO
1
;
Ke-Qian YANG
Author Information
1. State Key Laboratoy of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Bacterial Proteins;
biosynthesis;
genetics;
Carrier Proteins;
biosynthesis;
genetics;
Escherichia coli;
genetics;
metabolism;
Genetic Vectors;
genetics;
Green Fluorescent Proteins;
biosynthesis;
genetics;
isolation & purification;
Humans;
Recombinant Fusion Proteins;
biosynthesis;
genetics;
isolation & purification;
Repressor Proteins;
biosynthesis;
chemistry;
genetics;
Scyphozoa;
chemistry;
Spectrometry, Fluorescence;
Tetracycline;
metabolism;
Tetracycline Resistance
- From:
Chinese Journal of Biotechnology
2005;21(1):97-101
- CountryChina
- Language:Chinese
-
Abstract:
Tetracycline repressor gene (tetR) from E. coli transposon Tn10 was fused in frame with green fluorescent protein gene (gfp) from jellyfish Aequorea Victoria on an E. coli expression vector and the fusion protein (TR::GFP) was purified. The binding of TR::GFP with tetracycline (tc) was demonstrated by nitrocellulose filter binding assay. TR::GFP also maintained the fluorescence property of GFP. Most significantly, fluorescence emission intensity of TR::GFP increased by 2-fold in the presence of tc, from 1.132 to 2.214, while those of GFP and TetR showed little change under similar conditions. The results indicated TR::GFP possesses characteristics of a tetracycline biosensor.
