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Three aspartic acid residues of polygalacturonase‐inhibiting protein (PGIP) from Phaseolus vulgaris are critical for inhibition of Fusarium phyllophilum PG
Author(s) -
Spinelli F.,
Mariotti L.,
Mattei B.,
Salvi G.,
Cervone F.,
Caprari C.
Publication year - 2009
Publication title -
plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 1435-8603
DOI - 10.1111/j.1438-8677.2008.00175.x
Subject(s) - biology , pichia pastoris , mutant , biochemistry , pectinase , mutagenesis , elicitor , aspergillus niger , site directed mutagenesis , aspergillus oryzae , enzyme , gene , recombinant dna
Polygalacturonase‐inhibiting proteins (PGIPs) are plant cell wall proteins that specifically inhibit the activity of endo polygalacturonases (PGs) produced by fungi during the infection process. The interaction with PGIPs limits the destructive potential of PGs and may trigger plant defence responses through the release of elicitor active oligogalacturonides. In order to pinpoint the residues of PvPGIP2 from Phaseolus vulgaris involved in the interaction with PGs, we used site‐directed mutagenesis to mutate the residues D131, D157 and D203, and tested for the inhibitory activity of the mutant proteins expressed in Pichia pastoris against Fusarium phyllophilum and Aspergillus niger PGs. Here, we report that mutation of these residues affects the inhibition capacity of PvPGIP2 against F. phyllophilum PG.