Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Rhie, G.E. et al.

Manganese-containing superoxide dismutase and its gene from Candida albicans.

Mitochondrial manganese-containing superoxide dismutase was purified around 112-fold with an overall yield of 1.1% to apparent electrophoretic homogeneity from the dimorphic pathogenic fungus, Candida albicans. The molecular mass of the native enzyme was 106 kDa and the enzyme was composed of four identical subunits with a molecular mass of 26 kDa. The enzyme was not sensitive to either cyanide or hydrogen peroxide. The N-terminal amino acid sequence alignments (up to the 18th residue) showed that the enzyme has high similarity to the other eukaryotic manganese-containing superoxide dismutases. The gene sod2 encoding manganese-containing superoxide dismutase has been cloned using a product obtained from polymerase chain reaction. Sequence analysis of the sod2 predicted a manganese-containing superoxide dismutase that contains 234 amino acid residues with a molecular mass of 26173 Da, and displayed 57% sequence identity to the homologue of Saccharomyces cerevisiae. The deduced N-terminal 34 amino acid residues may serve as a signal peptide for mitochondrial translocation. Several regulatory elements such as stress responsive element and haem activator protein 2/3/4/5 complex binding sites were identified in the promoter region of sod2. Northern analysis with a probe derived from the cloned sod2 revealed a 0.94-kb band, which corresponds approximately to the expected size of mRNA deduced from sod2.[1]

References

Manganese-containing superoxide dismutase and its gene from Candida albicans. Rhie, G.E., Hwang, C.S., Brady, M.J., Kim, S.T., Kim, Y.R., Huh, W.K., Baek, Y.U., Lee, B.H., Lee, J.S., Kang, S.O. Biochim. Biophys. Acta (1999) [Pubmed]

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