Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system.

@article{Liu2005IncreaseOS,
  title={Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system.},
  author={Yang Liu and Tong-jin Zhao and Yong-bin Yan and Hai-Meng Zhou},
  journal={Protein expression and purification},
  year={2005},
  volume={44 2},
  pages={155-61}
}
Human protein disulfide isomerase (PDI) was selected as a fusion partner to construct a gene expression system to enhance the solubility of recombinant protein in Escherichia coli. DREBIII-1, a plant specific transcriptional factor, was found to mainly form inclusion bodies when expressed in either His-tagged or GST-fusion systems in E. coli. In contrast, when fused with PDI, the expressed DREBIII-1 was in a highly soluble and biologically active form. Two fusion proteins, HDP and HPD, were… CONTINUE READING