Efficient expression of the yeast metallothionein gene in Escherichia coli.

  title={Efficient expression of the yeast metallothionein gene in Escherichia coli.},
  author={T R Berka and A M Shatzman and Justin Zimmerman and James Strickler and Martin Goldstern Hajime Machida Ivo G. Rosenberg},
  journal={Journal of bacteriology},
  volume={170 1},
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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