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. 1988 Jan;170(1):21–26. doi: 10.1128/jb.170.1.21-26.1988

Efficient expression of the yeast metallothionein gene in Escherichia coli.

T Berka 1, A Shatzman 1, J Zimmerman 1, J Strickler 1, M Rosenberg 1
PMCID: PMC210600  PMID: 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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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