title: The Arabidopsis RESURRECTION1 gene regulates a novel antagonistic interaction in plant defense to biotrophs and necrotrophs.
abstract: We report a role for the Arabidopsis (Arabidopsis thaliana) RESURRECTION1 (RST1) gene in plant defense. The rst1 mutant exhibits enhanced susceptibility to the biotrophic fungal pathogen Erysiphe cichoracearum but enhanced resistance to the necrotrophic fungal pathogens Botrytis cinerea and Alternaria brassicicola. RST1 encodes a novel protein that localizes to the plasma membrane and is predicted to contain 11 transmembrane domains. Disease responses in rst1 correlate with higher levels of jasmonic acid (JA) and increased basal and B. cinerea-induced expression of the plant defensin PDF1.2 gene but reduced E. cichoracearum-inducible salicylic acid levels and expression of pathogenesis-related genes PR1 and PR2. These results are consistent with rst1's varied resistance and susceptibility to pathogens of different life styles. Cuticular lipids, both cutin monomers and cuticular waxes, on rst1 leaves were significantly elevated, indicating a role for RST1 in the suppression of leaf cuticle lipid synthesis. The rst1 cuticle exhibits normal permeability, however, indicating that the disease responses of rst1 are not due to changes in this cuticle property. Double mutant analysis revealed that the coi1 mutation (causing defective JA signaling) is completely epistatic to rst1, whereas the ein2 mutation (causing defective ethylene signaling) is partially epistatic to rst1, for resistance to B. cinerea. The rst1 mutation thus defines a unique combination of disease responses to biotrophic and necrotrophic fungi in that it antagonizes salicylic acid-dependent defense and enhances JA-mediated defense through a mechanism that also controls cuticle synthesis.
authors.affiliation: Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, Indiana 47907-2054, USA.
authors.forename: Hyung Gon
authors.initials: HG
authors.lastname: Mang
authors.forename: Kristin A
authors.initials: KA
authors.lastname: Laluk
authors.forename: Eugene P
authors.initials: EP
authors.lastname: Parsons
authors.forename: Dylan K
authors.initials: DK
authors.lastname: Kosma
authors.forename: Bruce R
authors.initials: BR
authors.lastname: Cooper
authors.forename: Hyeong Cheol
authors.initials: HC
authors.lastname: Park
authors.forename: Synan
authors.initials: S
authors.lastname: AbuQamar
authors.forename: Claudia
authors.initials: C
authors.lastname: Boccongelli
authors.forename: Saori
authors.initials: S
authors.lastname: Miyazaki
authors.forename: Federica
authors.initials: F
authors.lastname: Consiglio
authors.forename: Gabriele
authors.initials: G
authors.lastname: Chilosi
authors.forename: Hans J
authors.initials: HJ
authors.lastname: Bohnert
authors.forename: Ray A
authors.initials: RA
authors.lastname: Bressan
authors.forename: Tesfaye
authors.initials: T
authors.lastname: Mengiste
authors.forename: Matthew A
authors.initials: MA
authors.lastname: Jenks
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001419:Bacteria; D003517:Cyclopentanes / Q000378:metabolism; D005658:Fungi; D018506:Gene Expression Regulation, Plant / Q000276:immunology*; D008055:Lipids / Q000502:physiology; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D054883:Oxylipins / Q000378:metabolism; D010935:Plant Diseases / Q000276:immunology* / Q000382:microbiology; D019441:Plant Epidermis / Q000502:physiology
chemical_list: D029681:Arabidopsis Proteins; D003517:Cyclopentanes; D008055:Lipids; D008565:Membrane Proteins; D054883:Oxylipins; C544824:RST1 protein, Arabidopsis; C011006:jasmonic acid