New insights into the specificity and processivity of two novel pectinases from Verticillium dahliae

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Safran, Josip | Habrylo, Olivier | Cherkaoui, Mehdi | Lecomte, Sylvain | Voxeur, Aline | Pilard, Serge | Bassard, Solène | Pau-Roblot, Corinne | Mercadante, Davide | Pelloux, Jérôme | Sénéchal, Fabien

Edité par HAL CCSD ; Elsevier

International audience. Pectin, the major non-cellulosic component of primary cell wall can be degraded by polygalacturonases (PGs) and pectin methylesterases (PMEs) during pathogen attack on plants. We characterized two novel enzymes,VdPG2 and VdPME1, from the fungal plant pathogen Verticillium dahliae. VdPME1 was most active on citrus methylesterified pectin (55–70%) at pH 6 and a temperature of 40 °C, while VdPG2 was most active on polygalacturonic acid at pH 5 and a temperature of 50 °C. Using LC-MS/MS oligo profiling, and various pectins,the mode of action of VdPME1 and VdPG2 were determined. VdPME1 was shown to be processive, in accordance with the electrostatic potential of the enzyme. VdPG2 was identified asendo-PG releasing both methylesterified and non-methylesterified oligogalacturonides (OGs). Additionally, whenflax roots were used as substrate, acet-ylated OGs were detected. The comparisons of OGs released from Verticillium-susceptible and partially resistant flax cultivars identified new possible elicitor of plant defence responses.

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