Mitochondrial superoxide decreases yeast survival in stationary phase - PubMed (original) (raw)
. 1999 May 1;365(1):131-42.
doi: 10.1006/abbi.1999.1158.
Affiliations
- PMID: 10222047
- DOI: 10.1006/abbi.1999.1158
Mitochondrial superoxide decreases yeast survival in stationary phase
V D Longo et al. Arch Biochem Biophys. 1999.
Erratum in
- Arch Biochem Biophys 2000 May 1;377(1):213
Abstract
Yeast lacking mitochondrial superoxide dismutase (MnSOD) display shortened stationary-phase survival and provide a good model system for studying mitochondrial oxidative damage. We observed a marked decrease in respiratory function preceding stationary-phase death of yeast lacking MnSOD (sod2Delta). Agents (mitochondrial inhibitors) that are known to increase or decrease superoxide production in submitochondrial particles affected stationary-phase survival in a manner inversely correlated with their effects on superoxide production, implicating superoxide in this mitochondrial disfunction. Similar but less-dramatic effects were observed in wild-type yeast. The activities of certain mitochondrial enzymes were particularly affected. In sod2Delta yeast the activity of aconitase, a 4Fe-4S-cluster-containing enzyme located in the matrix, was greatly and progressively decreased as the cells established stationary phase. Succinate dehydrogenase activity also decreased in MnSOD mutants; cytochrome oxidase and ATPase activities did not. Aconitase could be reactivated by addition of materials required for cluster assembly (Fe3+ and a sulfur source), both in extracts and in vivo, indicating that inactivation of the enzyme was by disassembly of the cluster. Our results support the conclusion that superoxide is generated in the mitochondria in vivo and under physiological conditions and that MnSOD is the primary defense against this toxicity. When the balance between superoxide generation and MnSOD activity is disrupted, superoxide mediates iron release from mitochondrial iron-sulfur clusters, leading first to loss of mitochondrial function and then to death, independently of mtDNA damage. These results raise the possibility that similar processes may occur in higher eukaryotes.
Copyright 1999 Academic Press.
Similar articles
- Cloned prokaryotic iron superoxide dismutase protects yeast cells against oxidative stress depending on mitochondrial location.
Balzan R, Agius DR, Bannister WH. Balzan R, et al. Biochem Biophys Res Commun. 1999 Mar 5;256(1):63-7. doi: 10.1006/bbrc.1999.0285. Biochem Biophys Res Commun. 1999. PMID: 10066423 - Prolonged ethanol administration depletes mitochondrial DNA in MnSOD-overexpressing transgenic mice, but not in their wild type littermates.
Larosche I, Choumar A, Fromenty B, Lettéron P, Abbey-Toby A, Van Remmen H, Epstein CJ, Richardson A, Feldmann G, Pessayre D, Mansouri A. Larosche I, et al. Toxicol Appl Pharmacol. 2009 Feb 1;234(3):326-38. doi: 10.1016/j.taap.2008.11.004. Epub 2008 Nov 20. Toxicol Appl Pharmacol. 2009. PMID: 19063909 - Oxidative damage in the retinal mitochondria of diabetic mice: possible protection by superoxide dismutase.
Kanwar M, Chan PS, Kern TS, Kowluru RA. Kanwar M, et al. Invest Ophthalmol Vis Sci. 2007 Aug;48(8):3805-11. doi: 10.1167/iovs.06-1280. Invest Ophthalmol Vis Sci. 2007. PMID: 17652755 - Cross-compartment protection by SOD1.
Liochev SI, Fridovich I. Liochev SI, et al. Free Radic Biol Med. 2005 Jan 1;38(1):146-7. doi: 10.1016/j.freeradbiomed.2004.10.017. Free Radic Biol Med. 2005. PMID: 15589383 Review. - Respiratory function decline and DNA mutation in mitochondria, oxidative stress and altered gene expression during aging.
Wei YH, Wu SB, Ma YS, Lee HC. Wei YH, et al. Chang Gung Med J. 2009 Mar-Apr;32(2):113-32. Chang Gung Med J. 2009. PMID: 19403001 Review.
Cited by
- Mitochondrial superoxide dismutase Sod2 suppresses nuclear genome instability during oxidative stress.
Gupta SV, Campos L, Schmidt KH. Gupta SV, et al. Genetics. 2023 Oct 4;225(2):iyad147. doi: 10.1093/genetics/iyad147. Genetics. 2023. PMID: 37638880 Free PMC article. - Nab3 nuclear granule accumulation is driven by respiratory capacity.
Hutchinson KM, Hunn JC, Reines D. Hutchinson KM, et al. Curr Genet. 2022 Dec;68(5-6):581-591. doi: 10.1007/s00294-022-01248-w. Epub 2022 Aug 3. Curr Genet. 2022. PMID: 35922525 Free PMC article. - The Neuroprotective Effect of L-Carnitine against Glyceraldehyde-Induced Metabolic Impairment: Possible Implications in Alzheimer's Disease.
Magi S, Preziuso A, Piccirillo S, Giampieri F, Cianciosi D, Orciani M, Amoroso S. Magi S, et al. Cells. 2021 Aug 17;10(8):2109. doi: 10.3390/cells10082109. Cells. 2021. PMID: 34440878 Free PMC article. - Deciphering the mechanism by which the yeast Phaffia rhodozyma responds adaptively to environmental, nutritional, and genetic cues.
Flores-Cotera LB, Chávez-Cabrera C, Martínez-Cárdenas A, Sánchez S, García-Flores OU. Flores-Cotera LB, et al. J Ind Microbiol Biotechnol. 2021 Dec 23;48(9-10):kuab048. doi: 10.1093/jimb/kuab048. J Ind Microbiol Biotechnol. 2021. PMID: 34302341 Free PMC article. Review. - An energetics perspective on geroscience: mitochondrial protonmotive force and aging.
Berry BJ, Kaeberlein M. Berry BJ, et al. Geroscience. 2021 Aug;43(4):1591-1604. doi: 10.1007/s11357-021-00365-7. Epub 2021 Apr 17. Geroscience. 2021. PMID: 33864592 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases