Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli

Article Abstract:

Overexpression of the chaperonelike trigger factor of E. coli can prevent recombinant proteins from aggregating. Trigger factor correctly folded three recombinant proteins known to be susceptible to aggregation: mouse endostatin, human oxygen-regulated protein ORP150, and human lysozyme.

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Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and trnsported to the periplasm in Escherichia coli

Article Abstract:

Results show that periplasmic production and stabilization of horseradish peroxidase is influenced by Dsb proteins and calcium. Data indicate that total enzyme production increases severalfold by the overexpression of disulfide-bonded isomerase DsbC.

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Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEl-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli

Article Abstract:

DnaK-DnaJ-GrpE and GroEl-GroES containing chaperone coexpression plasmids were constructed and used to stabilize the assembly of recombinant proteins synthesized in the heterologous expression system of Escherichia coli. The plasmids were able to promote the synthesis of stable Cryj2, a Japanese cedar pollen allergen, in Escherichia coli. The functions of DnaK-DnaJ-GrpE and GroEl-GroES are distinct and synergistic.

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