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.

AtPME17 is a functional arabidopsis thaliana pectin methylesterase regulated by its PRO region that triggers PME activity in the resistance to botrytis cinerea / Del Corpo, D.; Fullone, M. R.; Miele, R.; Lafond, M.; Pontiggia, D.; Grisel, S.; Kieffer-Jaquinod, S.; Giardina, T.; Bellincampi, D.; Lionetti, V.. - In: MOLECULAR PLANT PATHOLOGY. - ISSN 1464-6722. - 21:12(2020), pp. 1620-1633. [10.1111/mpp.13002]

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

Del Corpo D.;Fullone M. R.;Miele R.;Pontiggia D.;Bellincampi D.;Lionetti V.
2020

Abstract

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.
2020
arabidopsis thaliana; botrytis cinerea; cell wall integrity; pectin methylesterases; plant immunity
01 Pubblicazione su rivista::01a Articolo in rivista
AtPME17 is a functional arabidopsis thaliana pectin methylesterase regulated by its PRO region that triggers PME activity in the resistance to botrytis cinerea / Del Corpo, D.; Fullone, M. R.; Miele, R.; Lafond, M.; Pontiggia, D.; Grisel, S.; Kieffer-Jaquinod, S.; Giardina, T.; Bellincampi, D.; Lionetti, V.. - In: MOLECULAR PLANT PATHOLOGY. - ISSN 1464-6722. - 21:12(2020), pp. 1620-1633. [10.1111/mpp.13002]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1467444
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