Multiple Epoxide Hydrolases in Alternaria alternata f. sp. lycopersici and Their Relationship to Medium Composition and Host-Specific Toxin Production
AUTOR(ES)
Morisseau, Christophe
FONTE
American Society for Microbiology
RESUMO
The production of Alternaria alternata f. sp. lycopersici host-specific toxins (AAL toxins) and epoxide hydrolase (EH) activity were studied during the growth of this plant-pathogenic fungus in stationary liquid cultures. Media containing pectin as the primary carbon source displayed peaks of EH activity at day 4 and at day 12. When pectin was replaced by glucose, there was a single peak of EH activity at day 6. Partial characterization of the EH activities suggests the presence of three biochemically distinguishable EH activities. Two of them have a molecular mass of 25 kDa and a pI of 4.9, while the other has a molecular mass of 20 kDa and a pI of 4.7. Each of the EH activities can be distinguished by substrate preference and sensitivity to inhibitors. The EH activities present at day 6 (glucose) or day 12 (pectin) are concomitant with AAL toxin production.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=91353Documentos Relacionados
- Production of the Mycotoxin Fumonisin B1 by Alternaria alternata f. sp. lycopersici†
- âConidial production and reaction of Alternaria alternata f. sp. citri to plant extractsâ
- Maculosin, a host-specific phytotoxin for spotted knapweed from Alternaria alternata
- Host-Specific Effects of Toxin from the Rough Lemon Pathotype of Alternaria alternata on Mitochondria 1
- A longevity assurance gene homolog of tomato mediates resistance to Alternaria alternata f. sp. lycopersici toxins and fumonisin B1
