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.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Cadmium / metabolism
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Cloning, Molecular
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Copper / metabolism
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Escherichia coli / genetics*
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Escherichia coli / metabolism
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Gene Expression Regulation*
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Genes
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Genes, Bacterial
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Genes, Fungal*
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Metallothionein / biosynthesis
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Metallothionein / genetics*
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Metallothionein / isolation & purification
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Metallothionein / metabolism
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Plasmids
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / metabolism
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Zinc / metabolism
Substances
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Cadmium
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Copper
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Metallothionein
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Zinc