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http://purl.uniprot.org/citations/33029918http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33029918http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.org/dc/terms/identifier"doi:10.1111/mpp.13002"xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Grisel S."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Kieffer-Jaquinod S."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Giardina T."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Miele R."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Bellincampi D."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Lionetti V."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Lafond M."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Fullone M.R."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Pontiggia D."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/author"Del Corpo D."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/name"Mol Plant Pathol"xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/pages"1620-1633"xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/title"AtPME17 is a functional Arabidopsis thaliana pectin methylesterase regulated by its PRO region that triggers PME activity in the resistance to Botrytis cinerea."xsd:string
http://purl.uniprot.org/citations/33029918http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/33029918http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33029918
http://purl.uniprot.org/citations/33029918http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33029918
http://purl.uniprot.org/uniprot/#_O22149-mappedCitation-33029918http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33029918
http://purl.uniprot.org/uniprot/#_Q9FI23-mappedCitation-33029918http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33029918
http://purl.uniprot.org/uniprot/O22149http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33029918
http://purl.uniprot.org/uniprot/Q9FI23http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33029918