The Endo-β-1,4-Xylanase Xyn11A Is Required for Virulence in Botrytis cinerea
Author(s) -
Nélida Brito,
José J. Espino,
Celedonio González
Publication year - 2006
Publication title -
molecular plant-microbe interactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.565
H-Index - 153
eISSN - 1943-7706
pISSN - 0894-0282
DOI - 10.1094/mpmi-19-0025
Subject(s) - xylanase , xylan , hemicellulose , mutant , virulence , extracellular , gene , biochemistry , enzyme , botrytis cinerea , wild type , biology , cell wall , microbiology and biotechnology , xylose , glycoside hydrolase , chemistry , cellulose , botany , fermentation
Phytopathogenic fungi can degrade xylan, an abundant hemicellulose in plant cell walls, by the coordinate action of a group of extracellular enzymes. Among these, endo-beta-1,4-xylanases carry out the initial breakdown by cleaving internal bonds in the polymer backbone. We have isolated and characterized a gene, xyn11A, coding for an endo-beta-1,4-xylanase belonging to family 11 of glycosyl hydrolases. xyn11A was shown to be induced by xylan and repressed by glucose and to be expressed in planta. The disruption of xyn11A caused only a moderate decrease, about 30%, in the level of extracellular endo-beta-1-4-xylanase activity and in the growth rate, with beechwood xylan as the only carbon source. However, deletion of the gene had a more pronounced effect on virulence, delaying the appearance of secondary lesions and reducing the average lesion size by more than 70%. Reintroducing the wild-type gene into the mutant strains reversed this phenotype back to wild type.
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