title: Arabidopsis PECTIN METHYLESTERASEs contribute to immunity against Pseudomonas syringae.
abstract: Pectins, major components of dicot cell walls, are synthesized in a heavily methylesterified form in the Golgi and are partially deesterified by pectin methylesterases (PMEs) upon export to the cell wall. PME activity is important for the virulence of the necrotrophic fungal pathogen Botrytis cinerea. Here, the roles of Arabidopsis PMEs in pattern-triggered immunity and immune responses to the necrotrophic fungus Alternaria brassicicola and the bacterial hemibiotroph Pseudomonas syringae pv maculicola ES4326 (Pma ES4326) were studied. Plant PME activity increased during pattern-triggered immunity and after inoculation with either pathogen. The increase of PME activity in response to pathogen treatment was concomitant with a decrease in pectin methylesterification. The pathogen-induced PME activity did not require salicylic acid or ethylene signaling, but was dependent on jasmonic acid signaling. In the case of induction by A. brassicicola, the ethylene response factor, but not the MYC2 branch of jasmonic acid signaling, contributed to induction of PME activity, whereas in the case of induction by Pma ES4326, both branches contributed. There are 66 PME genes in Arabidopsis, suggesting extensive genetic redundancy. Nevertheless, selected pme single, double, triple and quadruple mutants allowed significantly more growth of Pma ES4326 than wild-type plants, indicating a role of PMEs in resistance to this pathogen. No decreases in total PME activity were detected in these pme mutants, suggesting that the determinant of immunity is not total PME activity; rather, it is some specific effect of PMEs such as changes in the pattern of pectin methylesterification.
authors.affiliation: Department of Plant Biology and Microbial and Plant Genomics Institute , University of Minnesota, Saint Paul, Minnesota 55108.
authors.forename: Gerit
authors.initials: G
authors.lastname: Bethke
authors.forename: Rachael E
authors.initials: RE
authors.lastname: Grundman
authors.forename: Suma
authors.initials: S
authors.lastname: Sreekanta
authors.forename: William
authors.initials: W
authors.lastname: Truman
authors.forename: Fumiaki
authors.initials: F
authors.lastname: Katagiri
authors.forename: Jane
authors.initials: J
authors.lastname: Glazebrook
mesh_terms: D000528:Alternaria / Q000472:pathogenicity / Q000502:physiology; D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics / Q000276:immunology* / Q000382:microbiology; D029681:Arabidopsis Proteins / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D003517:Cyclopentanes / Q000378:metabolism; D004951:Esterification; D018506:Gene Expression Regulation, Plant; D009154:Mutation / Q000235:genetics; D054883:Oxylipins / Q000378:metabolism; D010368:Pectins / Q000378:metabolism; D010935:Plant Diseases / Q000276:immunology / Q000382:microbiology; D057865:Plant Immunity / Q000276:immunology*; D044224:Pseudomonas syringae / Q000472:pathogenicity / Q000502:physiology*; D051192:Receptors, Pattern Recognition / Q000378:metabolism; D015854:Up-Regulation / Q000235:genetics
chemical_list: D029681:Arabidopsis Proteins; D003517:Cyclopentanes; D054883:Oxylipins; D051192:Receptors, Pattern Recognition; C011006:jasmonic acid; D010368:Pectins; D002265:Carboxylic Ester Hydrolases; C022323:pectinesterase