AI Article Synopsis
- The AbGst1 gene from the pathogenic fungus Alternaria brassicicola encodes a glutathione transferase, which was isolated from a culture treated with benzyl isothiocyanate.
- The protein (AbGst1p) shows significant similarity to glutathione transferases found in yeast, and its expression is enhanced by isothiocyanates and heavy metals, but not by superoxide-generating agents.
- When expressed in E. coli, AbGst1p demonstrated high activity with certain isothiocyanates but lacked peroxidase activity, and the gene's upregulation in plants suggests its role in detoxifying compounds during plant infections.
Article Abstract
The AbGst1 gene encoding a glutathione transferase from the necrotrophic pathogen Alternaria brassicicola was cloned from a benzyl isothiocyanate-treated conidial culture using differential display reverse transcription. The deduced amino-acid sequence of AbGst1p showed a significant degree of similarity to glutathione transferase-I from Saccharomyces cerevisiae and glutathione transferase-III from Schizosaccharomyces pombe. The transcription of AbGst1 was significantly enhanced by isothiocyanates, heavy metals and 1-chloro-2,4-dinitrobenzene. However, no significant transcript response was obtained with superoxide-generating menadione and paraquat. Recombinant AbGst1p expressed in Escherichia coli exhibited high transferase activity with allyl and benzyl isothiocyanates as substrate compared with 1-chloro-2,4-dinitrobenzene, but no peroxidase activity was detected. AbGst1 was upregulated in planta during the first day postinfection, suggesting the potential involvement of this enzyme in isothiocyanate detoxification mechanisms during host plant infection.
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| http://dx.doi.org/10.1111/j.1574-6968.2006.00223.x | DOI Listing |
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