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GintGRX1, the first characterized glomeromycotan glutaredoxin, is a multifunctional enzyme that responds to oxidative stress
Glutaredoxins (GRXs) are small proteins with glutathione-dependent disulfide oxidoreductase activity involved in cellular defense against oxidative stress. This work reports the identification and characterization of the first glomeromycotan dithiol glutaredoxin gene from the fungus Glomus intraradi...
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Published in: | Fungal genetics and biology 2009, Vol.46 (1), p.94-103 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
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Summary: | Glutaredoxins (GRXs) are small proteins with glutathione-dependent disulfide oxidoreductase activity involved in cellular defense against oxidative stress. This work reports the identification and characterization of the first glomeromycotan dithiol glutaredoxin gene from the fungus
Glomus intraradices. The corresponding gene, named
GintGRX1, shares high sequence similarity with previously described fungal GRXs. GintGRX1 contains the characteristic dithiol active site CPYC. By using a yeast expression system, we found that
GintGRX1 encodes a multifunctional protein with oxidoreductase, peroxidase and glutathione
S-transferase activity. GintGRX1 partially reverted sensitivity to superoxide radicals of the Δ
grx1Δgrx2
Saccharomyces cerevisiae strain.
GintGRX1 was transcriptionally regulated by paraquat but not by hydrogen peroxide. Copper induced an accumulation of reactive oxygen species in the extraradical mycelium of
G. intraradices and up-regulation of
GintGRX1 transcript levels. These data suggest a role for GintGRX1 in protecting the fungus against the oxidative damage induced directly by the superoxide anion or indirectly by copper. |
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ISSN: | 1087-1845 1096-0937 |
DOI: | 10.1016/j.fgb.2008.09.013 |