CRS5 encodes a metallothionein-like protein in Saccharomyces cerevisiae

Protection from copper toxicity in the bakers' yeast Saccharomyces cerevisiae involves the action of a copper binding metallothionein encoded by the CUP1 locus. To identify additional factors contributing to copper ion homeostasis and detoxification, we screened a genomic library for genes that...

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Bibliographic Details
Published in:The Journal of biological chemistry 1994-10, Vol.269 (41), p.25295-25302
Main Authors: Culotta, V C, Howard, W R, Liu, X F
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Carrier Proteins
COBRE
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
Copper - metabolism
Copper - pharmacology
CUIVRE
DNA-Binding Proteins - metabolism
Dose-Response Relationship, Drug
Drug Resistance, Microbial
GENE
Gene Deletion
Gene Expression Regulation, Fungal
GENES
Genes, Fungal - genetics
Homeostasis
METALLOPROTEINE
Metallothionein - genetics
METALPROTEINAS
Molecular Sequence Data
PROTEINAS AGLUTINANTES
PROTEINE DE LIAISON
Regulatory Sequences, Nucleic Acid - genetics
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - drug effects
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins
SECUENCIA NUCLEICA
Sequence Analysis, DNA
Sequence Homology, Amino Acid
SEQUENCE NUCLEIQUE
Suppression, Genetic
Transcription Factors - metabolism
Transformation, Genetic
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Summary:Protection from copper toxicity in the bakers' yeast Saccharomyces cerevisiae involves the action of a copper binding metallothionein encoded by the CUP1 locus. To identify additional factors contributing to copper ion homeostasis and detoxification, we screened a genomic library for genes that confer high levels of copper resistance to yeast strains lacking CUP1. This screen led to the identification of the CRS5 (copper-resistant suppressor) gene. By sequence analyses, CRS5 encodes a small molecular weight cysteine-rich protein with an amino acid sequence bearing all the features of a eukaryotic metallothionein. The CRS5 polypeptide exhibits a striking similarity to a number of mammalian and invertebrate metallothioneins, yet shares surprisingly little homology with CUP1. In yeast, CRS5 is expressed as a 0.5-kilobase mRNA that is regulated both by copper ions and by oxidative stress, and expression is dependent upon ACE1, a copper and DNA binding transcription factor also known to regulate CUP1. Deletion of the chromosomal CRS5 locus was found to increase cellular sensitivity to copper, but not cadmium, toxicity. These studies support an important role for the CRS5 metallothionein-like protein in copper homeostasis and detoxification.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)47246-8