The sequence encoding a superoxide dismutase (SOD) was isolated from the cDNA library of a zinc-tolerant strain of the ericoid mycorrhizal fungus Oidiodendron maius, grown under zinc-stress conditions. Sequence homology to other SODs strongly suggests that it is a copper- and zinc-containing SOD. Functional complementation assays showed that the gene confers increased tolerance to zinc and copper stress to a Cu,ZnSOD-defective yeast mutant. Monitoring of transcript and protein levels following zinc stress suggests that OmSOD1 expression is controlled at the transcriptional level. The OmSod1 protein was found both in the cell extract and in the growth medium of viable fungal cultures. This is the first characterization of an extracellular Cu,ZnSOD in a mycorrhizal fungus. In nature, the presence of OmSod1 in the extracellular environment may also extend the protective role of this enzyme to the plant symbiont. This may be of particular interest from the perspective of using mycorrhizal fungi in bioremediation programmes.
Cu,Zn superoxide dismutase and zinc stress in the metal-tolerant ericoid mycorrhizal fungus Oidiodendron maius Zn
MARTINO, ELENA;MURAT FURMINIEUX, Claude Fernand;CHIAPELLO, Marco;PEROTTO, Silvia
2009-01-01
Abstract
The sequence encoding a superoxide dismutase (SOD) was isolated from the cDNA library of a zinc-tolerant strain of the ericoid mycorrhizal fungus Oidiodendron maius, grown under zinc-stress conditions. Sequence homology to other SODs strongly suggests that it is a copper- and zinc-containing SOD. Functional complementation assays showed that the gene confers increased tolerance to zinc and copper stress to a Cu,ZnSOD-defective yeast mutant. Monitoring of transcript and protein levels following zinc stress suggests that OmSOD1 expression is controlled at the transcriptional level. The OmSod1 protein was found both in the cell extract and in the growth medium of viable fungal cultures. This is the first characterization of an extracellular Cu,ZnSOD in a mycorrhizal fungus. In nature, the presence of OmSod1 in the extracellular environment may also extend the protective role of this enzyme to the plant symbiont. This may be of particular interest from the perspective of using mycorrhizal fungi in bioremediation programmes.File | Dimensione | Formato | |
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