| Literature DB >> 3275610 |
T Berka1, A Shatzman, J Zimmerman, J Strickler, M Rosenberg.
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.Entities:
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Year: 1988 PMID: 3275610 PMCID: PMC210600 DOI: 10.1128/jb.170.1.21-26.1988
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490