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  4. Molecular Characterization of a Novel Lipase-Like Pathogen-Inducible Gene Family of Arabidopsis
 
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Molecular Characterization of a Novel Lipase-Like Pathogen-Inducible Gene Family of Arabidopsis

Auteur(s)
Jakab, Gabor
Editeur(s)
Manrique, Amapola
Zimmerli, Laurent
Métraux, Jean-Pierre
Mauch-Mani, Brigitte 
Institut de biologie 
Date de parution
2003
In
Plant Physiology, American Society of Plant Biologists, 2003/132/4/2230-2239
Résumé
In a differential screening between Arabidopsis plants pretreated with the resistance-inducer ß-aminobutyric acid and untreated control plants, we have identified a gene encoding a novel lipase-like protein, <i>PRLIP1</i>. The abundance of <i>PRLIP1</i> mRNAs in Arabidopsis leaves was up-regulated by application of ß-aminobutyric acid, salicylic acid (SA), and ethylene as well as by various pathogens. Induction of <i>PRLIP1</i> depended on a functioning SA and ethylene signal transduction pathway but was independent of jasmonate signaling. This novel pathogenesis-related (<i>PR</i>) gene of Arabidopsis belongs to a gene family consisting of six (<i>PRLIP1, PRLIP2, PRLIP4, PRLIP5, PRLIP6</i>, and <i>PRLIP7</i>) closely related members in tandem position on chromosome 5. Among these genes, <i>PRLIP2</i> also was induced in leaves by SA and infections by pathogens but on a much lower level than <i>PRLIP1</i>. The <i>PRLIP1</i> family showed a tissue-specific expression pattern. Both <i>PRLIP1</i> and <i>PRLIP2</i> were specifically expressed in leaves and siliques, <i>PRLIP1</i> additionally in stems and flowers. The expression of <i>PRLIP6</i> and <i>PRLIP4</i> was root specific, whereas mRNA of <i>PRLIP5</i> and <i>PRLIP7</i> were not detected in any of these tissues. The more distantly related genes <i>PRLIP3, PRLIP9</i>, and <i>PRLIP8</i> were found on chromosomes 2, 4, and 5, respectively. The expression level of <i>PRLIP3</i> was checked and found constitutive during the different stress conditions tested. The <i>PRLIP1</i> gene was overexpressed in <i>Escherichia coli</i>, and the resulting <i>PRLIP1</i> protein showed esterase activity on <i>p</i>-nitrophenyl-butyrate and allowed the growth of the bacteria on lipidic substrates such as Tween20 or Tween80.
URI
https://libra.unine.ch/handle/123456789/11488
DOI
10.1104/pp.103.025312
Autre version
http://dx.doi.org/10.1104/pp.103.025312
Type de publication
Resource Types::text::journal::journal article
Dossier(s) à télécharger
 main article: Jakab_Gabor_-_Molecular_Characterization_of_a_Novel_Lipase-Like_20110728163205-OU.pdf (882.42 KB)
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