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J. Biol. Chem., Vol. 276, Issue 47, 43784-43791, November 23, 2001
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From the We report here that in addition to a cytoplasmic
copper-zinc-containing superoxide dismutase (SOD) and a mitochondrial
manganese-containing SOD, Candida albicans expresses a
third SOD gene (SOD3). The deduced amino acid
sequence contains all of the motifs found in previously characterized
manganese-containing SODs, except the presence of a mitochondrial
transit peptide. Recombinant Sod3p expressed and purified from
Escherichia 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 a Saccharomyces cerevisiae mutant lacking the cytoplasmic copper-zinc-containing SOD. Northern blot analyses showed that the transcription of
SOD3 is induced neither 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.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF416340.
Candida albicans Expresses an Unusual Cytoplasmic
Manganese-containing Superoxide Dismutase (SOD3 Gene
Product) upon the Entry and during the Stationary Phase*
§,§,, and§¶
Département de Biochimie et
Microbiologie and the § Centre de Recherche, sur la
Structure, la Fonction et l'Ingénierie des Protéines,
Université Laval, Québec G1K 7P4, Canada
*
This work was supported in part by grants from the Natural
Sciences and Engineering Research Council (to Y. B.), the Medical Research Council (to N. D.), and the Fonds de la Recherche en Santé du Québec (to N. D. and Y. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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