Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress.

Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. Research Abstract Details 

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Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. Abstract Text:

Elena Milgrom,Heba Diab,Frank Middleton,Patricia M Kane,

Yeast mutants lacking vacuolar proton-translocating ATPase (V-ATPase) subunits (vma mutants) were sensitive to several different oxidants in a recent genomic screen (Thorpe, G. W., Fong, C. S., Alic, N., Higgins, V. J., and Dawes, I. W. (2004) Proc. Natl. Acad. Sci. U. S. A. 101, 6564-6569). We confirmed that mutants lacking a V(1) subunit (vma2Delta), V(o) subunit, or either of the two V(o) a subunit isoforms are acutely sensitive to H(2)O(2) and more sensitive to menadione and diamide than wild-type cells. The vma2Delta mutant contains elevated levels of reactive oxygen species and high levels of oxidative protein damage even in the absence of an applied oxidant, suggesting an endogenous source of oxidative stress. vma2Delta mutants lacking mitochondrial DNA showed neither improved growth nor decreased sensitivity to peroxide, excluding respiration as the major source of the endogenous reactive oxygen species in the mutant. Double mutants lacking both VMA2 and components of the major cytosolic defense systems exhibited synthetic sensitivity to H(2)O(2). Microarray analysis comparing wild-type and vma2Delta mutant cells grown at pH 5, permissive conditions for the vma2Delta mutant, indicated high level up-regulation of several iron uptake and metabolism genes that are part of the Aft1/Aft2 regulon. TSA2, which encodes an isoform of the cytosolic thioredoxin peroxidase, was strongly induced, but other oxidative stress defense systems were not induced. The results indicate that V-ATPase activity helps to protect cells from endogenous oxidative stress.

Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. Publishing Authors By Initials

E Milgrom,H Diab,F Middleton,PM Kane,

For similar enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: adenosine triphosphatases: proton-translocating atpases: vacuolar proton-translocating atpases research abstracts see: enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: adenosine triphosphatases: proton-translocating atpases: vacuolar proton-translocating atpases research

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Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 7125-36

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 10

MONTH: 01

YEAR: 2007

Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. Keywords Mesh Terms:

KEYWORDS: Vacuolar Proton-Translocating ATPases

MESH TERMS: physiology

Chemical & Substance for Abstract: Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. Information

Substance Name: CUP5 protein, S cerevisiae

Registry Number: EC 3.6.3.14

Grant and Affiliation Information for Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress.

AFFILIATION: Department of Biochemistry, SUNY Upstate Medical University, Syracuse, New York 13210, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01-GM50322

ACRONYM: GM

MEDLINETA: J Biol Chem

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