Open AccessAn endo‐polygalacturonase (PG) of Fusarium moniliforme escaping inhibition by plant polygalacturonase‐inhibiting proteins (PGIPs) provides new insights into the PG–PGIP interaction
Author(s) -
Sella Luca,
Castiglioni Carla,
Roberti Serena,
D'Ovidio Renato,
Favaron Francesco
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/j.femsle.2004.09.019
Subject(s) - pectinase , enzyme , peptide sequence , biochemistry , fusarium , biology , gene isoform , amino acid , microbiology and biotechnology , chemistry , gene , botany
Polygalacturonase‐inhibiting proteins (PGIPs) are plant defence molecules inhibiting the activity of fungal endo‐polygalacturonases (endo‐PGs). We found that soybean and bean PGIPs inhibited the endo‐PG activity produced by the isolate FC‐10 of Fusarium moniliforme but not the enzyme activity produced by the isolate PD of F. moniliforme . The bean PGIP proved to be ineffective against all the PG isoforms produced by the PD isolate. Deduced amino acid sequence comparison between PGs from PD, FC‐10 and 62264 isolates identified the structural regions of the enzyme possibly related to its resistance to PGIP inhibition. These include one region at the N‐terminal portion of the enzyme and a few single amino acid substitutions along the entire sequence, two of which surrounding the active site.