Increased solubility of glutathione S-transferase-p16 (GST-p16) fusion protein by co-expression of chaperones groes and groel in Escherichia coli

Abstract

Human cdk (cyclin dependent kinase) inhibitor p16 was fused with glutathione S-transferase (GST) and the GST-p16 fusion protein is under the control of T7 promoter. When expressed in E. coli BL21(DE3), most products existed in the form of insoluble inclusion bodies. When co-expressed with molecular chaperones E. coli GroESL, most GST-p16 products accumulated in the soluble form with a 5-6 fold increase in solubility. When co-produced with human protein disulfide isomerase (PDI), there was no improvement in the solubility of GST-p16 fusion protein.