SOD2/YHR008C Summary Help

Standard Name SOD2 1
Systematic Name YHR008C
Feature Type ORF, Verified
Description Mitochondrial manganese superoxide dismutase, protects cells against oxygen toxicity; phosphorylated (2, 3, 4 and see Summary Paragraph)
Name Description SuperOxide Dismutase 2
Chromosomal Location
ChrVIII:123590 to 122889 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: 12 cM
Gene Ontology Annotations All SOD2 GO evidence and references
  View Computational GO annotations for SOD2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Pathways
Mutant phenotypes All SOD2 Phenotype evidence and references
Classical genetics
null
overexpression
Large-scale survey
null
Resources
interactions All SOD2 Interaction evidence and references
87 total interaction(s) for 75 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 8
  • Affinity Capture-RNA: 5
  • Co-crystal Structure: 1
  • PCA: 2
  • Reconstituted Complex: 2
Genetic Interactions
  • Dosage Rescue: 4
  • Negative Genetic: 32
  • Phenotypic Enhancement: 8
  • Phenotypic Suppression: 7
  • Positive Genetic: 5
  • Synthetic Growth Defect: 6
  • Synthetic Lethality: 2
  • Synthetic Rescue: 5
Resources
Expression Summary
histogram
Resources
Protein Information All SOD2 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVIII:123590 to 122889 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: 12 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..702 123590..122889 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001050
SUMMARY PARAGRAPH for SOD2

SOD2 encodes a manganese-superoxide dismutase (MnSOD) that is localized to the mitochondrial matrix and is involved in oxygen radical detoxification. S. cerevisiae also carries a copper-zinc superoxide dismutase, Sod1p, which is located in both the cytosol and the mitochondrial intermembrane space. SODs catalyze the breakdown of the superoxide radical, O2-, to an oxygen molecule (dioxygen) and hydrogen peroxide (5, 6). Strains with null mutations in SOD2 are hypersensitive to high concentrations of oxygen and ethanol (2, 7), but grow normally in atmospheric oxygen and die rapidly in stationary phase. sod2 mutations are also associated with defects such as sensitivity to oxidative stress, defective sporulation and a high mutation rate (2, 8, 9, 10). SOD1 and SOD2 are among the first genes to be implicated in the chronological aging of yeast (5, 6, 11). Deletion of SOD1 or both SOD1 and SOD2 dramatically reduces the chronological and replicative life span of yeast (8), while overexpression of both SOD1 and SOD2 extends survival but does not affect metabolic rates (12).

Sod2p is a homotetramer with one atom of manganese per subunit (13, 14) which is acquired after import into the mitochondrial matrix. The specific manganese chaperone Mtm1p activates the apo-Sod2p by delivering the manganese ion to Sod2p (15). Another metal ion transporter protein, Smf2p, regulates the availability of manganese to Sod2p (16). SOD2 expression is repressed in the absence of heme and by low levels of intracellular cAMP levels. SOD2 expression is positively regulated by the heme-dependent activator Hap 2-3-4-5 complex and the heme binding transcription activator, Hap1p. Transcription of SOD2 involves proteins that sense oxygen or by-products of respiration since paraquat, a superoxide radical producer, and oxygen can induce SOD2 transcription (17, 18).

Mn-SOD is a highly conserved gene. Inactivation of the mouse mitochondrial form of SOD results in dilated cardiomyopathy, hepatic lipid accumulation, and early neonatal death and other biochemical abnormalities that have features similar to mitochondrial myopathy, Friedreich ataxia, and 3-hydroxy-3-methylglutaryl-CoA lyase (HMGCL) deficiency (19).

Last updated: 2008-06-25

References cited on this page View Complete Literature Guide for SOD2
1) Gralla, E. and Kosman, D.  (1992) Personal Communication, Mortimer Map Edition 11
2) van Loon AP, et al.  (1986) A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen. Proc Natl Acad Sci U S A 83(11):3820-4
3) Saffi J, et al.  (2006) Antioxidant activity of L-ascorbic acid in wild-type and superoxide dismutase deficient strains of Saccharomyces cerevisiae. Redox Rep 11(4):179-84
4) Reinders J, et al.  (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906
5) Steinman HM  (1980) The amino acid sequence of copper-zinc superoxide dismutase from bakers' yeast. J Biol Chem 255(14):6758-65
6) Bermingham-McDonogh O, et al.  (1988) The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity. Proc Natl Acad Sci U S A 85(13):4789-93
7) Costa V, et al.  (1993) Acquisition of ethanol tolerance in Saccharomyces cerevisiae: the key role of the mitochondrial superoxide dismutase. Arch Biochem Biophys 300(2):608-14
8) Longo VD, et al.  (1996) Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo. J Biol Chem 271(21):12275-80
9) Longo VD, et al.  (1999) Mitochondrial superoxide decreases yeast survival in stationary phase. Arch Biochem Biophys 365(1):131-42
10) Liu XF, et al.  (1992) Yeast lacking superoxide dismutase. Isolation of genetic suppressors. J Biol Chem 267(26):18298-302
11) Culotta VC, et al.  (1995) A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering. J Biol Chem 270(50):29991-7
12) Fabrizio P and Longo VD  (2003) The chronological life span of Saccharomyces cerevisiae. Aging Cell 2(2):73-81
13) Luk E, et al.  (2005) Manganese activation of superoxide dismutase 2 in the mitochondria of Saccharomyces cerevisiae. J Biol Chem 280(24):22715-20
14) Ravindranath SD and Fridovich I  (1975) Isolation and characterization of a manganese-containing superoxide dismutase from yeast. J Biol Chem 250(15):6107-12
15) Luk E, et al.  (2003) Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae requires MTM1, a member of the mitochondrial carrier family. Proc Natl Acad Sci U S A 100(18):10353-7
16) Luk EE and Culotta VC  (2001) Manganese superoxide dismutase in Saccharomyces cerevisiae acquires its metal co-factor through a pathway involving the Nramp metal transporter, Smf2p. J Biol Chem 276(50):47556-62
17) Flattery-O'Brien JA, et al.  (1997) Stationary-phase regulation of the Saccharomyces cerevisiae SOD2 gene is dependent on additive effects of HAP2/3/4/5- and STRE-binding elements. Mol Microbiol 23(2):303-12
18) Pinkham JL, et al.  (1997) Heme regulates SOD2 transcription by activation and repression in Saccharomyces cerevisiae. Curr Genet 31(4):281-91
19) Melov S, et al.  (1999) Mitochondrial disease in superoxide dismutase 2 mutant mice. Proc Natl Acad Sci U S A 96(3):846-51