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Effects of co-expression of liver X receptor β-ligand binding domain with its partner, retinoid X receptor α-ligand binding domain, on their solubility and biological activity in Escherichia coli



Effects of co-expression of liver X receptor β-ligand binding domain with its partner, retinoid X receptor α-ligand binding domain, on their solubility and biological activity in Escherichia coli



Journal of Microbiology and Biotechnology 25(2): 247-254



In this presentation, I describe the expression and purification of the recombinant liver X receptor β-ligand binding domain proteins in E. coli using a commercially available double cistronic vector, pACYCDuet-1, to express the receptor heterodimer in a single cell as the soluble form. I describe here the expression and characterization of a biologically active heterodimer composed of the liver X receptor β-ligand binding domain and retinoid X receptor α-ligand binding domain. Although many of these proteins were previously seen to be produced in E. coli as insoluble aggregates or "inclusion bodies", I show here that as a form of heterodimer they can be made in soluble forms that are biologically active. This suggests that co-expression of the liver X receptor β-ligand binding domain with its binding partner improves the solubility of the complex and probably assists in their correct folding, thereby functioning as a type of molecular chaperone.

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Accession: 052860045

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PMID: 25223325


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