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  • Title: The expression in Escherichia coli of a synthetic gene coding for the precursor of papain is prevented by its own putative signal sequence.
    Author: Vernet T, Tessier DC, Laliberté F, Dignard D, Thomas DY.
    Journal: Gene; 1989 Apr 30; 77(2):229-36. PubMed ID: 2666263.
    Abstract:
    A 1048-bp gene coding for prepropapain was assembled from chemically synthesized oligodeoxyribonucleotides and cloned into a variety of Escherichia coli expression plasmids. We observed loss of plasmid when the preproP gene was expressed in E. coli either as the native precursor or fused at the C terminus of the first 592 amino acids (aa) of beta-galactosidase (beta Gal). Deletion of the putative 26-aa signal peptide (pre-region) increased plasmid stability. The level of maintenance for the different plasmid constructs correlated with the level of expression detected by immunoblotting. Constitutive expression of the beta Gal-propapain fusion generated insoluble granules in a protease-deficient E. coli host. The fusion protein was easily purified to near homogeneity by differential solubilization of the granules.
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