Increased solubility of glutathione S-transferase-P16 (GST-p16) fusion protein by co-expression of chaperones groes and groel in Escherichia coli.
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 coproduced with human protein disulfide isomerase (PDI), there was no improvement in the solubility of GST-p16 fusion protein.
Luo
Z H
ZH
Department of Biochemistry, Nanjing University, People's Republic of China.
Hua
Z C
ZC
D018835:Chaperonin 10 / Q000096:biosynthesis* / Q000235:genetics; D018834:Chaperonin 60 / Q000096:biosynthesis* / Q000235:genetics; D019941:Cyclin-Dependent Kinase Inhibitor p16 / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005982:Glutathione Transferase / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D006801:Humans; D002479:Inclusion Bodies; D008970:Molecular Weight; D011401:Promoter Regions, Genetic; D019704:Protein Disulfide-Isomerases / Q000235:genetics; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry; D012995:Solubility
D018835:Chaperonin 10; D018834:Chaperonin 60; D019941:Cyclin-Dependent Kinase Inhibitor p16; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase; D019704:Protein Disulfide-Isomerases