title: Spatio-temporal expression of patatin-like lipid acyl hydrolases and accumulation of jasmonates in elicitor-treated tobacco leaves are not affected by endogenous levels of salicylic acid.
abstract: We have previously isolated three tobacco genes (NtPat) encoding patatin-like proteins, getting rapidly induced during the hypersensitive response (HR) to tobacco mosaic virus, in advance to jasmonate accumulation. NtPAT enzymes are lipid acyl hydrolases that display high phospholipase A2 (PLA2) activity and may mobilize fatty acid precursors of oxylipins. Here, we performed a detailed study of NtPat gene regulation under various biotic and abiotic stresses. PLA2 activity was poorly induced in response to drought, wounding, reactive oxygen intermediates, salicylic acid (SA) or methyl-jasmonate (MJ) whereas the ethylene (ET) precursor, 1-aminocyclopropane-1-carboxylic acid (ACC), provoked a moderate induction. In contrast, PLA2 activity was strongly induced when ACC was combined with MJ, and in response to the bacterium Erwinia carotovora or to the fungus Botrytis cinerea, as well as to treatment with beta-megaspermin, a cell death-inducing protein elicitor. A simplified system based on the infiltration of beta-megaspermin into leaves was used to dissect the spatio-temporal activation of PLA2 activity with regards to the accumulation of jasmonates and to the influence of endogenous SA. NtPat-encoded PLA2 activity was rapidly induced in the infiltrated zone before the appearance of cell death and with some delay in the surrounding living cells. A massive accumulation of 12-oxo-phytodienoic and jasmonic acids occurred in the elicitor-infiltrated zone, but only low levels were detectable outside this area. A similar picture was found in SA-deficient plants, showing that in tobacco, accumulation of jasmonates is not affected by the concomitant HR-induced build-up of endogenous SA. Finally, ET-insensitive plants showed a weakened induction of PLA2 activity outside the elicitor-infiltrated tissue.
authors.affiliation: Institut de Biologie Moléculaire des Plantes (IBMP) du CNRS, Université Louis Pasteur, 12 rue du Général Zimmer, Strasbourg Cedex, 67084 France.
authors.forename: Sandrine
authors.initials: S
authors.lastname: Dhondt
authors.forename: Guillaume
authors.initials: G
authors.lastname: Gouzerh
authors.forename: Axel
authors.initials: A
authors.lastname: Müller
authors.forename: Michel
authors.initials: M
authors.lastname: Legrand
authors.forename: Thierry
authors.initials: T
authors.lastname: Heitz
mesh_terms: D003517:Cyclopentanes / Q000378:metabolism* / Q000494:pharmacology; D004190:Disasters; D004790:Enzyme Induction / Q000187:drug effects; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D017343:Genes, Plant / Q000235:genetics; D054883:Oxylipins; D010741:Phospholipases A / Q000235:genetics / Q000378:metabolism*; D054467:Phospholipases A2; D010935:Plant Diseases / Q000235:genetics / Q000382:microbiology; D018515:Plant Leaves / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology; D012459:Salicylates / Q000378:metabolism*; D013997:Time Factors; D014026:Nicotiana / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism* / Q000382:microbiology
chemical_list: D003517:Cyclopentanes; D054883:Oxylipins; D012459:Salicylates; C011006:jasmonic acid; D010741:Phospholipases A; D054467:Phospholipases A2