Research Report

Molecular cloning, expression, and purification of a urease accessory protein UreG of Arabidopsis thaliana  

Kou Jing1 , Testuo Takano2 , Liu Shenkui1 , Bu Yuanyuan1
1 Key Laboratory of Saline-alkali Vegetation Ecology Restoration in Oil Field (SAVER), Ministry of Education, Alkali Soil Natural Environmental Science Center (ASNESC), Northeast Forestry University, Harbin, 150040, China
2 Asian Natural Environmental Science Center (ANESC), the University of Tokyo, Tokyo 188-0002, Japan
Author    Correspondence author
Molecular Soil Biology, 2016, Vol. 7, No. 6   doi: 10.5376/msb.2016.07.0006
Received: 05 May, 2016    Accepted: 01 Jun., 2016    Published: 08 Jun., 2016
© 2016 BioPublisher Publishing Platform
This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:

Kou J., Takano T., Liu S., and Bu Y.Y., 2016, Molecular Cloning, Expression, and Purification of a Urease Accessory Protein UreG of Arabidopsis thaliana, Molecular Soil Biology, 7(6): 1-6 (doi: 10.5376/msb.2016.07.0006)


UreG is one of the accessory proteins of urease in plants. In this study, a gene encoding an UreG consisting of 363 amino acids from Arabidopsis thaliana was isolated. The AtUreG gene was expressed in Escherichia coli BL21 as a GST fusion protein. The GST-AtUreG fusion protein was induced and purified under the optimized culturing conditions of 0.2 mM IPTG and 25℃ for 5 h. Western blot analysis using an anti-GST antibody showed that the GST-AtUreG fusion protein was not degraded.

AtUreG; Protein expression; Arabidopsis thaliana
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