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Secretion of mouse-metallothionein by engineered E. coli cells in metal-enriched culture media.

Heterologous Escherichia coli expression systems were designed and assayed for the synthesis of functional mouse metallothionein (MT) as a secreted fusion protein. MT secretion was compared among different systems, and the optimum vector/host/medium combination was tested for metal removal. In this case, the Cu content of the medium decreased by up to 34% after growth of recombinant bacteria. The potential use of these genetically-engineered bacteria for water bioremediation is discussed as an alternative to cytoplasmic MT or membrane-bound MT heterologous expression systems.