A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering

Valeria L Culotta, Hung Dong Joh, Su Ju Lin, Kimberly Hudak Slekar, Jeffrey Strain

Research output: Contribution to journalArticle

Abstract

The copper toxicity of yeast lacking the CUP1 metallothionein is suppressed by overexpression of the CRS4 gene. We now demonstrate that CRS4 is equivalent to SOD1, encoding copper/zinc superoxide dismutase (SOD). While overexpression of SOD1 enhanced copper resistance, a deletion of SOD1, but not SOD2 (encoding manganese SOD), conferred an increased sensitivity toward copper. This role of SOD1 in copper buffering appears unrelated to its superoxide scavenging activity, since the enzyme protected against copper toxicity in anaerobic as well as aerobic conditions. The distinct roles of SOD1 in copper and oxygen radical homeostasis could also be separated genetically: the pmr1, bsd2, and ATX1 genes that suppress oxygen toxicity in sod1 mutants failed to suppress the copper sensitivity of these cells. The Saccharomyces cerevisiae SOD1 gene is transcriptionally induced by copper and the ACE1 transactivator, and we demonstrate here that this induction of SOD1 promotes protection against copper toxicity but is not needed for the SOD1- protection against oxygen free radicals. Collectively, these findings indicate that copper/zinc SOD functions in the homeostasis of copper via mechanisms distinct from superoxide scavenging.

Original languageEnglish (US)
Pages (from-to)29991-29997
Number of pages7
JournalJournal of Biological Chemistry
Volume270
Issue number50
DOIs
StatePublished - Dec 15 1995

Fingerprint

Yeast
Superoxide Dismutase
Saccharomyces cerevisiae
Zinc
Copper
Toxicity
Genes
Scavenging
Superoxides
Reactive Oxygen Species
Homeostasis
Oxygen
Trans-Activators
Metallothionein
Free Radicals
Yeasts

ASJC Scopus subject areas

  • Biochemistry

Cite this

A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering. / Culotta, Valeria L; Joh, Hung Dong; Lin, Su Ju; Slekar, Kimberly Hudak; Strain, Jeffrey.

In: Journal of Biological Chemistry, Vol. 270, No. 50, 15.12.1995, p. 29991-29997.

Research output: Contribution to journalArticle

Culotta, Valeria L ; Joh, Hung Dong ; Lin, Su Ju ; Slekar, Kimberly Hudak ; Strain, Jeffrey. / A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering. In: Journal of Biological Chemistry. 1995 ; Vol. 270, No. 50. pp. 29991-29997.
@article{b1186a9fb58b4e94a35298ba7350ae5e,
title = "A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering",
abstract = "The copper toxicity of yeast lacking the CUP1 metallothionein is suppressed by overexpression of the CRS4 gene. We now demonstrate that CRS4 is equivalent to SOD1, encoding copper/zinc superoxide dismutase (SOD). While overexpression of SOD1 enhanced copper resistance, a deletion of SOD1, but not SOD2 (encoding manganese SOD), conferred an increased sensitivity toward copper. This role of SOD1 in copper buffering appears unrelated to its superoxide scavenging activity, since the enzyme protected against copper toxicity in anaerobic as well as aerobic conditions. The distinct roles of SOD1 in copper and oxygen radical homeostasis could also be separated genetically: the pmr1, bsd2, and ATX1 genes that suppress oxygen toxicity in sod1 mutants failed to suppress the copper sensitivity of these cells. The Saccharomyces cerevisiae SOD1 gene is transcriptionally induced by copper and the ACE1 transactivator, and we demonstrate here that this induction of SOD1 promotes protection against copper toxicity but is not needed for the SOD1- protection against oxygen free radicals. Collectively, these findings indicate that copper/zinc SOD functions in the homeostasis of copper via mechanisms distinct from superoxide scavenging.",
author = "Culotta, {Valeria L} and Joh, {Hung Dong} and Lin, {Su Ju} and Slekar, {Kimberly Hudak} and Jeffrey Strain",
year = "1995",
month = "12",
day = "15",
doi = "10.1074/jbc.270.50.29991",
language = "English (US)",
volume = "270",
pages = "29991--29997",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "50",

}

TY - JOUR

T1 - A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering

AU - Culotta, Valeria L

AU - Joh, Hung Dong

AU - Lin, Su Ju

AU - Slekar, Kimberly Hudak

AU - Strain, Jeffrey

PY - 1995/12/15

Y1 - 1995/12/15

N2 - The copper toxicity of yeast lacking the CUP1 metallothionein is suppressed by overexpression of the CRS4 gene. We now demonstrate that CRS4 is equivalent to SOD1, encoding copper/zinc superoxide dismutase (SOD). While overexpression of SOD1 enhanced copper resistance, a deletion of SOD1, but not SOD2 (encoding manganese SOD), conferred an increased sensitivity toward copper. This role of SOD1 in copper buffering appears unrelated to its superoxide scavenging activity, since the enzyme protected against copper toxicity in anaerobic as well as aerobic conditions. The distinct roles of SOD1 in copper and oxygen radical homeostasis could also be separated genetically: the pmr1, bsd2, and ATX1 genes that suppress oxygen toxicity in sod1 mutants failed to suppress the copper sensitivity of these cells. The Saccharomyces cerevisiae SOD1 gene is transcriptionally induced by copper and the ACE1 transactivator, and we demonstrate here that this induction of SOD1 promotes protection against copper toxicity but is not needed for the SOD1- protection against oxygen free radicals. Collectively, these findings indicate that copper/zinc SOD functions in the homeostasis of copper via mechanisms distinct from superoxide scavenging.

AB - The copper toxicity of yeast lacking the CUP1 metallothionein is suppressed by overexpression of the CRS4 gene. We now demonstrate that CRS4 is equivalent to SOD1, encoding copper/zinc superoxide dismutase (SOD). While overexpression of SOD1 enhanced copper resistance, a deletion of SOD1, but not SOD2 (encoding manganese SOD), conferred an increased sensitivity toward copper. This role of SOD1 in copper buffering appears unrelated to its superoxide scavenging activity, since the enzyme protected against copper toxicity in anaerobic as well as aerobic conditions. The distinct roles of SOD1 in copper and oxygen radical homeostasis could also be separated genetically: the pmr1, bsd2, and ATX1 genes that suppress oxygen toxicity in sod1 mutants failed to suppress the copper sensitivity of these cells. The Saccharomyces cerevisiae SOD1 gene is transcriptionally induced by copper and the ACE1 transactivator, and we demonstrate here that this induction of SOD1 promotes protection against copper toxicity but is not needed for the SOD1- protection against oxygen free radicals. Collectively, these findings indicate that copper/zinc SOD functions in the homeostasis of copper via mechanisms distinct from superoxide scavenging.

UR - http://www.scopus.com/inward/record.url?scp=0038153078&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038153078&partnerID=8YFLogxK

U2 - 10.1074/jbc.270.50.29991

DO - 10.1074/jbc.270.50.29991

M3 - Article

C2 - 8530401

AN - SCOPUS:0038153078

VL - 270

SP - 29991

EP - 29997

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 50

ER -