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Pectin is synthesized in a highly methylesterified form in the Golgi cisternae and partially de‐methylesterified in muro by pectin methylesterases (PMEs).  Arabidopsis thaliana  produces a local and strong induction of PME activity during the infection of the necrotrophic fungus  Botrytis cinerea . AtPME17 is a putative  A. thaliana  PME highly induced in response to  B. cinerea . Here, a fine tuning of AtPME17 expression by different defence hormones was identified. Our genetic evidence demonstrates that AtPME17 strongly contributes to the pathogen‐induced PME activity and resistance against  B. cinerea  by triggering jasmonic acid–ethylene‐dependent  PDF1.2  expression. AtPME17 belongs to group 2 isoforms of PMEs characterized by a PME domain preceded by an N‐terminal PRO region. However, the biochemical evidence for AtPME17 as a functional PME is still lacking and the role played by its PRO region is not known. Using the  Pichia pastoris  expression system, we demonstrate that AtPME17 is a functional PME with activity favoured by an increase in pH. AtPME17 performs a blockwise pattern of pectin de‐methylesterification that favours the formation of egg‐box structures between homogalacturonans. Recombinant AtPME17 expression in  Escherichia coli  reveals that the PRO region acts as an intramolecular inhibitor of AtPME17 activity.

molecular plant pathology

AtPME17 is a functional  Arabidopsis thaliana  pectin methylesterase regulated by its PRO region that triggers PME activity in the resistance to  Botrytis cinerea