Efficient expression of the yeast metallothionein gene in Escherichia coli.

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Berka T,Shatzman A,Zimmerman J,Strickler J,Rosenberg M

doi

10.1128/jb.170.1.21-26.1988

subject

Has Abstract

pub_date

1988-01-01 00:00:00

pages

21-6

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

170

pub_type

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