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Updated: Jul 12, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
Overproduction of mouse estrogen receptor alpha-ligand binding domain decreases bacterial growth
Swati Ghosh1, Mahendra Kumar Thakur
1Biochemistry and Molecular Biology Laboratory, Center of Advanced Study in Zoology, Banaras Hindu University, Varanasi, 221005, India.
Abstract:
Escherichia coli (E. coli) is the most widely used prokaryotic host system for the synthesis of recombinant proteins. The overproduction of recombinant proteins is sometimes lethal to the host cells. In the present study, we expressed the ligand binding domain (LBD) of mouse estrogen receptor alpha (mouse ERalpha) using an expression vector (pIVEX) in E. coli BL21(DE3) and examined the effect of production of this protein on bacterial growth. The expressed protein was immunologically detected as a 30 kD histidine-tagged protein in the soluble part of the bacterial lysate. The overproduction of mouse ERalpha-LBD, as reflected by total protein content and expression pattern, resulted in the decrease of bacterial growth.
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