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Published on April 28, 2006; 10.1104/pp.106.076950

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Received January 14, 2006
Returned for revision February 16, 2006
Accepted April 19, 2006

POLYGALACTURONASE-INHIBITING PROTEIN (PGIP) INTERACTS WITH PECTIN THROUGH A BINDING SITE FORMED BY FOUR CLUSTERED RESIDUES OF ARGININE AND LYSINE

S. Spadoni , O. Zabotina , A. Di Matteo , J.D. Mikkelsen , F. Cervone , De Lorenzo G. , B. Mattei *, and D. Bellincampi

* Corresponding author; email: benedetta.mattei{at}uniroma1.it.

Polygalacturonase-inhibiting protein (PGIP) is a cell wall protein that inhibits fungal polygalacturonases (PGs) and retards the invasion of plant tissues by phytopathogenic fungi. Here we report the interaction of two PGIP isoforms from Phaseolus vulgaris (PvPGIP1 and PvPGIP2) with both polygalacturonic acid (PGA) and cell wall fractions containing uronic acids. We identify in the 3-D structure of the PvPGIP2 a motif of four clustered arginines and lysine (R183, R206, K230, R252) responsible for this binding. The four residues were mutated and the protein variants were expressed in Pichia pastoris. The ability of both wild type and mutated proteins to bind pectins was investigated by affinity chromatography. Single mutations impaired the binding and double mutations abolished the interaction, thus indicating that the four clustered residues form the pectin-binding site. Remarkably, the binding of PGIP to pectin is displaced in vitro by PGs, suggesting that PGIP interacts with pectin and PGs through overlapping although not identical regions. The specific interaction of PGIP with PGA may be strategic to protect pectins from the degrading activity of fungal PGs.




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