Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 343770
Title Endopolygalacturonases from Botrytis cinerea: biochemical properties and interaction with inhibiting proteins
Author(s) Krooshof, G.H.; Joosten, R.; Kester, H.C.M.; Kars, I.; Kan, J. van; Benen, J.A.E.
Source In: Book of Abstracts XXIII Fungal Genetics Conference, Pacific Grove, California, USA, 15-20 March 2005 - p. 197 - 197.
Department(s) Microbiological Laboratory
Laboratory of Phytopathology
EPS-2
Publication type Abstract in scientific journal or proceedings
Publication year 2005
Abstract The phytopathogen Botrytis cinerea harbours at least six endopolygalacturonase-encoding (Bcpg) genes of which Bcpg1 and Bcpg2 are required for full virulence. The endopolygalacturonase (BcPG) enzymes degrade pectin, enabling the fungus to breach the plant cell wall. We expressed five BcPG isozymes in Pichia pastoris, purified them and studied biochemical properties, such as pH optimum, mode of action, and substrate specificity in detail. BcPG3 shows a rather unusual, broad pH optimum and is the only isozyme fully active at pH 3.5. Polygalacturonic acid is a poor substrate for BcPG1 and BcPG4 as compared to BcPG2, BcPG3, and BcPG6. In contrast to BcPG1, 2, and 4, BcPG3 and BcPG6 show extreme processive behaviour on oligogalacturonides longer than four GalpA residues. Only BcPG3 and BcPG6 are able to hydrolyse GalpA dimers. Since PG activity is important for fungal virulence, the BcPGs are interesting targets for disease control. Therefore, a range of plant extracts was screened to identify potent polygalacturonase-inhibiting proteins (PGIPs). PGIPs from different plant sources have been purified and their interaction with the BcPG isozymes have been investigated using different techniques. Results on the mode of inhibition and binding will be presented.
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