Literature DB >> 8299153

Regulation of Saccharomyces cerevisiae catalase gene expression by copper.

P Lapinskas1, H Ruis, V Culotta.   

Abstract

Treatment of Saccharomyces cerevisiae cells with copper induces the activity of Cu/Zn superoxide dismutase (SOD) and catalase. To understand the level at which Cu regulates catalase, the expression of the S. cerevisiae CTA1 (encoding the peroxisomal catalase A) and CTT1 (encoding the cytosolic catalase T) genes was monitored as a function of Cu treatment. Copper was found to specifically induce transcription of CTT1, but not CTA1, mRNA. Moreover, genetic and biochemical studies demonstrate that this induction is independent of the ACE1 Cu trans-activator controlling the expression of yeast Cu/Zn SOD and metallothionein genes. Copper regulation of CTT1 thus appears to represent a novel metal regulatory pathway in S. cerevisiae cells.

Entities:  

Mesh：

Substances：

Year:  1993        PMID： 8299153     DOI： 10.1007/BF00351846

Source DB:  PubMed          Journal:  Curr Genet        ISSN： 0172-8083            Impact factor:   3.886


  27 in total

1.  Copper and the ACE1 regulatory protein reversibly induce yeast metallothionein gene transcription in a mouse extract.

Authors:  V C Culotta; T Hsu; S Hu; P Fürst; D Hamer
Journal:  Proc Natl Acad Sci U S A       Date:  1989-11       Impact factor: 11.205

2.  Preparation of high molecular weight RNA.

Authors:  K Köhrer; H Domdey
Journal:  Methods Enzymol       Date:  1991       Impact factor: 1.600

Review 3.  An overview of the relationship between oxidative stress and chemical carcinogenesis.

Authors:  M A Trush; T W Kensler
Journal:  Free Radic Biol Med       Date:  1991       Impact factor: 7.376

4.  Heat shock factor-independent heat control of transcription of the CTT1 gene encoding the cytosolic catalase T of Saccharomyces cerevisiae.

Authors:  R Wieser; G Adam; A Wagner; C Schüller; G Marchler; H Ruis; Z Krawiec; T Bilinski
Journal:  J Biol Chem       Date:  1991-07-05       Impact factor: 5.157

5.  Activation and induction by copper of Cu/Zn superoxide dismutase in Saccharomyces cerevisiae. Presence of an inactive proenzyme in anaerobic yeast.

Authors:  F Galiazzo; M R Ciriolo; M T Carrì; P Civitareale; L Marcocci; F Marmocchi; G Rotilio
Journal:  Eur J Biochem       Date:  1991-03-28

Review 6.  DNA damage and oxygen radical toxicity.

Authors:  J A Imlay; S Linn
Journal:  Science       Date:  1988-06-03       Impact factor: 47.728

7.  Isolation and sequence of the gene for actin in Saccharomyces cerevisiae.

Authors:  R Ng; J Abelson
Journal:  Proc Natl Acad Sci U S A       Date:  1980-07       Impact factor: 11.205

8.  Oxygen-independent induction of enzyme activities related to oxygen metabolism in yeast by copper.

Authors:  F Galiazzo; A Schiesser; G Rotilio
Journal:  Biochim Biophys Acta       Date:  1988-04-14

9.  Evidence for co-regulation of Cu,Zn superoxide dismutase and metallothionein gene expression in yeast through transcriptional control by copper via the ACE 1 factor.

Authors:  M T Carri; F Galiazzo; M R Ciriolo; G Rotilio
Journal:  FEBS Lett       Date:  1991-01-28       Impact factor: 4.124

10.  The CUP2 gene product regulates the expression of the CUP1 gene, coding for yeast metallothionein.

Authors:  J Welch; S Fogel; C Buchman; M Karin
Journal:  EMBO J       Date:  1989-01       Impact factor: 11.598
View more
  3 in total

1.  Isolation and characterization of a laccase gene from Podospora anserina.

Authors:  J Fernández-Larrea; U Stahl
Journal:  Mol Gen Genet       Date:  1996-10-16

2.  Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasaemic Saccharomyces cerevisiae.

Authors:  S Izawa; Y Inoue; A Kimura
Journal:  Biochem J       Date:  1996-11-15       Impact factor: 3.857

3.  Dual targeting of yeast catalase A to peroxisomes and mitochondria.

Authors:  Ventsislava Y Petrova; Diane Drescher; Anna V Kujumdzieva; Manfred J Schmitt
Journal:  Biochem J       Date:  2004-06-01       Impact factor: 3.857
  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.