COPPER METALLOTHIONEIN OF YEAST, STRUCTURE OF THE GENE, AND REGULATION OF EXPRESSION
COPPER METALLOTHIONEIN OF YEAST, STRUCTURE OF THE GENE, AND REGULATION OF EXPRESSION
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DOI:
10.1073/pnas.81.11.3332
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发表时间:
1984-01-01
期刊:
影响因子:
--
通讯作者:
CROOKE, ST
中科院分区:
文献类型:
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作者:
BUTT, TR;STERNBERG, EJ;CROOKE, ST
Addition of Cu to yeast [Saccharomyces cerevisiae] cells leads to the induction of a low MW, cysteine-rich protein that binds Cu. This protein, termed copper chelatin or thionein, is related to the metallothionein family of proteins that are induced in response to Cd and Zn in vertebrate cells. Structure of the yeast Cu-binding protein was determined by DNA sequence analysis of the gene. Although the 6573 dalton yeast protein is substantially divergent from vertebrate metallothioneins, the arrangement of 12 cysteine residues, which is a hallmark of metal-binding proteins, is partially conserved. The regulatory DNA sequence of the gene was analyzed by fusing it with the Escherichia coli galactokinase gene and assaying the levels of enzyme activity in yeast in response to Cu. Transcriptional activation has a specific requirement for Cu. Zn, Cd and Au were unable to regulate the galactokinase activity. The yeast copper metallothionein regulatory sequences represent a previously unreported class of yeast promoter that is regulated by Cu.