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Polygalacturonase-Inhibiting Proteins Can Function as Activators of Polygalacturonase

August 2004 , Volume 17 , Number  8
Pages  888 - 894

G. Kemp , 1 L. Stanton , 1 C. W. Bergmann , 1 R. P. Clay , 2 P. Albersheim , 1 and A. Darvill 1

1Complex Carbohydrate Research Center and Department of Biochemistry and Molecular Biology, University of Georgia, 315 Riverbend Road, Athens, Georgia 30602-4712, U.S.A.; 2Department of Biology, University of West Georgia, 1600 Maple St, Carrolton, Georgia, 30118, U.S.A.


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Accepted 1 April 2004.

The interaction between fungal endopolygalacturonases (EPGs) and polygalacturonase-inhibiting proteins (PGIPs) found in plant cell walls has been well established. The typical EPG/PGIP interaction is characterized by high affinity, reversibility, and a 1:1 stoichiometry that results in lowering the catalytic rate of a particular endopolygalacturonase by up to 99.7%. Various EPG and PGIP isoforms and glycoforms have been isolated and characterized, and combinations of EPGs and PGIPs demonstrate a range of enzyme inhibition. EPG/PGIP interactions have prompted many researchers to suspect the involvement of these proteins in the production of specific signals (oligosaccharins) during plant pathogenesis. We have recently reported on initial studies in our laboratory indicating that, for certain EPG/PGIP combinations, the specific activity of EPG is increased beyond that characteristic of the enzyme alone. In this paper, we rpesent a detailed analysis of the product of the interaction of native Phaseolus vulgaris PGIP-2 with five EPGs from Aspergillus niger, namely PGI, PGII, PGA, PGB, and PGC in the presence of homogalacturonan. We demonstrate that for PGA and PGC, the interaction with PGIP-2 may result in either inhibition or activation in a manner that is pH dependent. This data suggests the need for a reevaluation of the conventional description applied to PGIPs; suggestions include polygalacturonase-binding protein and polygalacturonase-modulating protein.


Additional keywords: plant defense, protein-protein interaction.

© 2004 The American Phytopathological Society