title: The elicitation of a systemic resistance by Pseudomonas putida BTP1 in tomato involves the stimulation of two lipoxygenase isoforms.
abstract: BACKGROUND
  Some non-pathogenic rhizobacteria called Plant Growth Promoting Rhizobacteria (PGPR) possess the capacity to induce in plant defense mechanisms effective against pathogens. Precedent studies showed the ability of Pseudomonas putida BTP1 to induce PGPR-mediated resistance, termed ISR (Induced Systemic Resistance), in different plant species. Despite extensive works, molecular defense mechanisms involved in ISR are less well understood that in the case of pathogen induced systemic acquired resistance.
  
  
  RESULTS
  We analyzed the activities of phenylalanine ammonia-lyase (PAL) and lipoxygenase (LOX), key enzymes of the phenylpropanoid and oxylipin pathways respectively, in tomato treated or not with P. putida BTP1. The bacterial treatment did not stimulate PAL activity and linoleate-consuming LOX activities. Linolenate-consuming LOX activity, on the contrary, was significantly stimulated in P. putida BTP1-inoculated plants before and two days after infection by B. cinerea. This stimulation is due to the increase of transcription level of two isoforms of LOX: TomLoxD and TomLoxF, a newly identified LOX gene. We showed that recombinant TomLOXF preferentially consumes linolenic acid and produces 13-derivative of fatty acids. After challenging with B. cinerea, the increase of transcription of these two LOX genes and higher linolenic acid-consuming LOX activity were associated with a more rapid accumulation of free 13-hydroperoxy-octadecatrienoic and 13-hydroxy-octadecatrienoic acids, two antifungal oxylipins, in bacterized plants.
  
  
  CONCLUSIONS
  In addition to the discovery of a new LOX gene in tomato, this work is the first to show differential induction of LOX isozymes and a more rapid accumulation of 13-hydroperoxy-octadecatrienoic and 13-hydroxy-octadecatrienoic acids in rhizobacteria mediated-induced systemic resistance.
authors.affiliation: Laboratory of Plant Molecular Biology and Biotechnology, Faculty of Sciences, Department of Life Sciences, University of Liège, Boulevard du Rectorat, 27, Liège, Belgium.
authors.forename: Martin
authors.initials: M
authors.lastname: Mariutto
authors.forename: Francéline
authors.initials: F
authors.lastname: Duby
authors.forename: Akram
authors.initials: A
authors.lastname: Adam
authors.forename: Charlotte
authors.initials: C
authors.lastname: Bureau
authors.forename: Marie-Laure
authors.initials: ML
authors.lastname: Fauconnier
authors.forename: Marc
authors.initials: M
authors.lastname: Ongena
authors.forename: Philippe
authors.initials: P
authors.lastname: Thonart
authors.forename: Jacques
authors.initials: J
authors.lastname: Dommes
mesh_terms: D000595:Amino Acid Sequence; D004790:Enzyme Induction; D015971:Gene Expression Regulation, Enzymologic; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant / Q000235:genetics; D007113:Immunity, Innate; D007527:Isoenzymes / Q000378:metabolism; D019787:Linoleic Acid / Q000378:metabolism; D008084:Lipoxygenase / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D018551:Solanum lycopersicum / Q000201:enzymology* / Q000235:genetics / Q000382:microbiology*; D008969:Molecular Sequence Data; D054883:Oxylipins / Q000378:metabolism; D010650:Phenylalanine Ammonia-Lyase / Q000235:genetics / Q000378:metabolism; D010802:Phylogeny; D010935:Plant Diseases / Q000276:immunology* / Q000382:microbiology*; D016958:Pseudomonas putida / Q000502:physiology*; D013379:Substrate Specificity; D013997:Time Factors; D017962:alpha-Linolenic Acid / Q000378:metabolism
chemical_list: D007527:Isoenzymes; D054883:Oxylipins; D017962:alpha-Linolenic Acid; D019787:Linoleic Acid; C117433:13-lipoxygenase; D008084:Lipoxygenase; D010650:Phenylalanine Ammonia-Lyase