Efficient expression of the yeast metallothionein gene in Escherichia coli.
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.
Berka
T
T
Department of Molecular Genetics, Smith Kline & French Laboratories, Swedeland, Pennsylvania 19406.
Shatzman
A
A
Zimmerman
J
J
Strickler
J
J
Rosenberg
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D002104:Cadmium / Q000378:metabolism; D003001:Cloning, Molecular; D003300:Copper / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005786:Gene Expression Regulation; D005796:Genes; D005798:Genes, Bacterial; D005800:Genes, Fungal; D008668:Metallothionein / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D010957:Plasmids; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D015032:Zinc / Q000378:metabolism
D002104:Cadmium; D003300:Copper; D008668:Metallothionein; D015032:Zinc