Design of a solubilization pathway for recombinant polypeptides in vivo through processing of a bi-protein with a viral protease.

@article{PrezMartn1997DesignOA,
  title={Design of a solubilization pathway for recombinant polypeptides in vivo through processing of a bi-protein with a viral protease.},
  author={Jose Manuel P{\'e}rez-Mart{\'i}n and Ildefonso Cases and V{\'i}ctor de Lorenzo},
  journal={Protein engineering},
  year={1997},
  volume={10 6},
  pages={725-30}
}
An artificial maturation pathway for increasing the solubility in vivo of recombinant proteins overproduced in Escherichia coli is reported, which is based on the proteolytic processing of viral polyproteins. The gene product of interest is expressed as a fusion to a heterologous moiety (i.e. the maltose binding protein, MalE) in order to increase the overall solubility of the hybrid. The hinge region between the two fusion partners contains a cleavage site for the NIa protein, a very specific… CONTINUE READING

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