Efficient expression of the yeast metallothionein gene in Escherichia coli
- 1 January 1988
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 170 (1) , 21-26
- https://doi.org/10.1128/jb.170.1.21-26.1988
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.This publication has 40 references indexed in Scilit:
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