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Titolo:
OXIDATIVE STRESS INDUCES HEAT-SHOCK FACTOR PHOSPHORYLATION AND HSF-DEPENDENT ACTIVATION OF YEAST METALLOTHIONEIN GENE-TRANSCRIPTION
Autore:
LIU HD; THIELE DJ;
Indirizzi:
UNIV MICHIGAN,SCH MED,DEPT BIOL CHEM ANN ARBOR MI 48109 UNIV MICHIGAN,SCH MED,DEPT BIOL CHEM ANN ARBOR MI 48109
Titolo Testata:
Genes & development
fascicolo: 5, volume: 10, anno: 1996,
pagine: 592 - 603
SICI:
0890-9369(1996)10:5<592:OSIHFP>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
SACCHAROMYCES-CEREVISIAE; HYDROGEN-PEROXIDE; DNA-BINDING; SUPEROXIDE-DISMUTASE; TRANSITION-METALS; ESCHERICHIA-COLI; FACTOR CONTAINS; HSP70; EXPRESSION; RESPONSES;
Keywords:
METALLOTHIONEIN; HEAT SHOCK FACTOR; OXIDATIVE STRESS; SUPEROXIDE DISMUTASE; TRANSCRIPTION; MENADIONE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
63
Recensione:
Indirizzi per estratti:
Citazione:
H.D. Liu e D.J. Thiele, "OXIDATIVE STRESS INDUCES HEAT-SHOCK FACTOR PHOSPHORYLATION AND HSF-DEPENDENT ACTIVATION OF YEAST METALLOTHIONEIN GENE-TRANSCRIPTION", Genes & development, 10(5), 1996, pp. 592-603

Abstract

Metallothioneins (MTs) are a class of low-molecular-weight, cysteine-rich metal-binding proteins that function in metal detoxification and oxidative stress protection. We demonstrate that transcription of the Saccharomyces cerevisiae MT gene CUP1 is strongly activated by the superoxide anion generator menadione. This activation is exacerbated in astrain lacking the gene encoding Cu, Zn superoxide dismutase (SOD1). CUP1 transcriptional activation by oxidative stress is dependent on a functional CUP1 promoter heat shock element (HSE) and the carboxy-terminal trans-activation domain of heat shock transcription factor (HSF). Furthermore, protection against oxidative stress conferred by CUP1 ina sod1 Delta strain requires HSF-mediated CUP1 transcription. Although in response to heat, HSE-mediated CUP1 transcription and HSF phosphorylation are transient, both CUP1 gene expression and HSF phosphorylation are sustained in response to oxidative stress. Moreover, the patterns of tryptic phosphopeptides resolved from HSF derived from cells subjected to heat shock or oxidative stress are distinct. These results demonstrate that transcription of the S. cerevisiae metallothionein gene under conditions of oxidative stress is mediated by HSF and that inresponse to distinct activation stimuli, HSF is differentially phosphorylated in a manner that parallels metallothionein gene transcription.

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Documento generato il 28/09/20 alle ore 05:32:24