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  • Title: Efficient expression of the yeast metallothionein gene in Escherichia coli.
    Author: Berka T, Shatzman A, Zimmerman J, Strickler J, Rosenberg M.
    Journal: J Bacteriol; 1988 Jan; 170(1):21-6. PubMed ID: 3275610.
    Abstract:
    The yeast metallothionein gene CUP1 was cloned into a bacterial expression system to achieve efficient, controlled expression of the stable, unprocessed protein product. The Escherichia coli-synthesized yeast metallothionein bound copper, cadmium, and zinc, indicating that the protein was functional. Furthermore, E. coli cells expressing CUP1 acquired a new, inducible ability to selectively sequester heavy metal ions from the growth medium.
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