GrainGenes Reference Report: MPM-13-1041
Reference
MPM-13-1041
Title
Stagonospora avenae secretes multiple enzymes that hydrolyze oat leaf saponins
Journal
Molecular Plant Microbe Interactions
Year
2000
Volume
13
Pages
1041-1052
Author
Morrissey JP Wubben JP Osbourn AE
Abstract
Summary: The phytopathogenic fungus Stagonospora avenae is able to infect oat leaves despite the presence of avenacoside saponins in the leaf tissue. In response to pathogen attack, avenacosides are converted into 26-desglucoavenacosides (26-DGAs), which possess antifungal activity. These molecules are comprised of a steroidal backbone linked to a branched sugar chain consisting of one alpha-L-rhamnose and two (avenacoside A) or three (avenacoside B) beta-D-glucose residues. Isolates of the fungus that are pathogenic to oats are capable of sequential hydrolysis of the sugar residues from the 26-DGAs. Degradation is initiated by removal of the L-rhamnose, which abolishes antifungal activity. The D-glucose residues are then hydrolyzed by beta-glucosidase activity. A comprehensive analysis of saponin-hydrolyzing activities was undertaken, and it was established that S. avenae isolate WAC1293 secretes three enzymes, one alpha- rhamnosidase and two beta-glucosidases, that carry out this hydrolysis. The major beta-glucosidase was purified and the gene encoding the enzyme cloned. The protein is similar to saponin-hydrolyzing enzymes produced by three other phytopathogenic fungi, Gaeumannomyces graminis, Septoria lycopersici, and Botrytis cinerea, and is a family 3 beta-glucosidase. The gene encoding the beta-glucosidase is expressed during infection of oat leaves but is not essential for pathogenicity
Keyword

GrainGenes is a product of the Agricultural Research Service of the US Department of Agriculture.
GrainGenes Reference Report: MPM-13-1041
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