title: Dissecting the beta-aminobutyric acid-induced priming phenomenon in Arabidopsis.
abstract: Plants treated with the nonprotein amino acid beta-aminobutyric acid (BABA) develop an enhanced capacity to resist biotic and abiotic stresses. This BABA-induced resistance (BABA-IR) is associated with an augmented capacity to express basal defense responses, a phenomenon known as priming. Based on the observation that high amounts of BABA induce sterility in Arabidopsis thaliana, a mutagenesis screen was performed to select mutants impaired in BABA-induced sterility (ibs). Here, we report the isolation and subsequent characterization of three T-DNA-tagged ibs mutants. Mutant ibs1 is affected in a cyclin-dependent kinase-like protein, and ibs2 is defective in AtSAC1b encoding a polyphosphoinositide phosphatase. Mutant ibs3 is affected in the regulation of the ABA1 gene encoding the abscisic acid (ABA) biosynthetic enzyme zeaxanthin epoxidase. To elucidate the function of the three IBS genes in plant resistance, the mutants were tested for BABA-IR against the bacterium Pseudomonas syringae pv tomato, the oomycete Hyaloperonospora parasitica, and BABA-induced tolerance to salt. All three ibs mutants were compromised in BABA-IR against H. parasitica, although to a different extent. Whereas ibs1 was reduced in priming for salicylate (SA)-dependent trailing necrosis, mutants ibs2 and ibs3 were affected in the priming for callose deposition. Only ibs1 failed to express BABA-IR against P. syringae, which coincided with a defect in priming for SA-inducible PR-1 gene expression. By contrast, ibs2 and ibs3 showed reduced BABA-induced tolerance to salt, which correlated with an affected priming for ABA-inducible gene expression. For all three ibs alleles, the defects in BABA-induced sterility and BABA-induced protection against P. syringae, H. parasitica, and salt could be confirmed in independent mutants. The data presented here introduce three novel regulatory genes involved in priming for different defense responses.
authors.affiliation: Department of Science, Laboratory of Biochemistry, University of Neuchâtel, 2007 Neuchâtel, Switzerland.
authors.forename: Jurriaan
authors.initials: J
authors.lastname: Ton
authors.forename: Gabor
authors.initials: G
authors.lastname: Jakab
authors.forename: Valérie
authors.initials: V
authors.lastname: Toquin
authors.forename: Victor
authors.initials: V
authors.lastname: Flors
authors.forename: Annalisa
authors.initials: A
authors.lastname: Iavicoli
authors.forename: Muriel N
authors.initials: MN
authors.lastname: Maeder
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Métraux
authors.forename: Brigitte
authors.initials: B
authors.lastname: Mauch-Mani
mesh_terms: D000483:Alleles; D000595:Amino Acid Sequence; D000613:Aminobutyrates / Q000494:pharmacology*; D017360:Arabidopsis / Q000187:drug effects* / Q000235:genetics / Q000502:physiology; D001483:Base Sequence; D018844:Cyclin-Dependent Kinases / Q000235:genetics / Q000378:metabolism; D004269:DNA, Bacterial / Q000235:genetics; D018744:DNA, Plant / Q000235:genetics; D004351:Drug Resistance / Q000235:genetics; D017343:Genes, Plant; D005809:Genes, Regulator; D008954:Models, Biological; D008969:Molecular Sequence Data; D009154:Mutation; D009868:Oomycetes / Q000472:pathogenicity; D009997:Osmotic Pressure; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000378:metabolism; D010935:Plant Diseases / Q000235:genetics / Q000382:microbiology; D030821:Plants, Genetically Modified; D044224:Pseudomonas syringae / Q000472:pathogenicity; D017386:Sequence Homology, Amino Acid; D012965:Sodium Chloride
chemical_list: D000613:Aminobutyrates; D004269:DNA, Bacterial; D018744:DNA, Plant; C036483:T-DNA; C047667:3-aminobutyric acid; D012965:Sodium Chloride; D010088:Oxidoreductases; C097153:zeaxanthin epoxidase; D018844:Cyclin-Dependent Kinases; D010744:Phosphoric Monoester Hydrolases
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