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Titolo:
CRS5 ENCODES A METALLOTHIONEIN-LIKE PROTEIN IN SACCHAROMYCES-CEREVISIAE
Autore:
CULOTTA VC; HOWARD WR; LIU XF;
Indirizzi:
JOHNS HOPKINS UNIV,SCH HYG & PUBL HLTH,DEPT ENVIRONM HLTH SCI,DIV TOXICOL SCI BALTIMORE MD 21205
Titolo Testata:
The Journal of biological chemistry
fascicolo: 41, volume: 269, anno: 1994,
pagine: 25295 - 25302
SICI:
0021-9258(1994)269:41<25295:CEAMPI>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION INITIATION SITES; ZINC SUPEROXIDE-DISMUTASE; DNA-BINDING PROTEIN; CUP2 GENE-PRODUCT; YEAST METALLOTHIONEIN; EXPRESSION; COPPER; ACE1; AMPLIFICATION; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
V.C. Culotta et al., "CRS5 ENCODES A METALLOTHIONEIN-LIKE PROTEIN IN SACCHAROMYCES-CEREVISIAE", The Journal of biological chemistry, 269(41), 1994, pp. 25295-25302

Abstract

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 asmall molecular weight cysteine-rich protein with an amino acid sequence bearing all the features of a eukaryotic metallothionein. The CRS5polypeptide 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 thatis 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 15:17:15