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Papers In Press, published online ahead of print September 18, 2001
Département de Biochimie et de Microbiologie, Université Laval, Québec, Québec G1K 7P4
Corresponding Author: yves.bourbonnais{at}rsvs.ulaval.ca
We report here that in addition to a cytoplasmic copper-zinc-containing superoxide dismutase (Cu/ZnSOD), and a mitochondrial manganese-containing SOD (MnSOD), C. albicans expresses a third SOD gene (SOD3). The deduced amino acid sequence contains all the motifs found in previously characterized MnSODs, except the presence of a mitochondrial transit peptide. Recombinant Sod3p expressed and purified from E. coli is a homotetramer with a subunit mass of 25.4 kDa. Mass absorption spectrometry detected the presence of both iron and manganese in purified Sod3p but, as determined by metal replacement experiments, the enzyme displays activity only when bound to manganese. Overexpression of SOD3 was shown to rescue the hypersensitivity to redox cycling agents of an S. cerevisiae mutant lacking the cytoplasmic Cu/ZnSOD. Northern blot analyses showed that the transcription of SOD3 is neither induced by the transition from the yeast to the mycelial form of C. albicans nor by drug-induced oxidative stress. In continuous cultures, the expression of SOD3 was strongly stimulated upon the entry and during the stationary phase, concomitantly with the repression of SOD1. We conclude that Sod3p is an atypical cytosolic manganese-containing superoxide dismutase that is involved in the protection of C. albicans against reactive oxygen species during the stationary phase.
J. Biol. Chem, 10.1074/jbc.M108095200
Submitted on August 22, 2001
Revised on September 13, 2001
Accepted on September 18, 2001
Candida albicans expresses an unusual cytoplasmic manganese-containing superoxide dismutase (SOD3 gene product) upon the entry and during the stationary phase
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