Three aspartic acid residues of polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris are critical for inhibition of Fusarium phyllophilum PG.
Polygalacturonase-inhibiting proteins (PGIPs) are plant cell wall proteins that specifically inhibit the activity of endopolygalacturonases (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.
Spinelli
F
F
Dipartimento di Biologia Vegetale, Università di Roma La Sapienza, Rome, Italy.
Mariotti
L
L
Mattei
B
B
Salvi
G
G
Cervone
F
F
Caprari
C
C
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000378:metabolism; D001483:Base Sequence; D005670:Fusarium / Q000201:enzymology*; D054884:Host-Pathogen Interactions; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D027805:Phaseolus / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011096:Polygalacturonase / Q000037:antagonists & inhibitors* / Q000378:metabolism
C081479:PGIP protein, plant; D010940:Plant Proteins; D001224:Aspartic Acid; D011096:Polygalacturonase