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.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Sellam A,Poupard P,Simoneau Pdoi
10.1111/j.1574-6968.2006.00223.xsubject
Has Abstractpub_date
2006-05-01 00:00:00pages
241-9issue
2eissn
0378-1097issn
1574-6968pii
FML223journal_volume
258pub_type
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