Document Detail


Plastid omega3-fatty acid desaturase-dependent accumulation of a systemic acquired resistance inducing activity in petiole exudates of Arabidopsis thaliana is independent of jasmonic acid.
MedLine Citation:
PMID:  18088304     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Systemic acquired resistance (SAR) is an inducible defense mechanism that is activated throughout the plant, subsequent to localized inoculation with a pathogen. The establishment of SAR requires translocation of an unknown signal from the pathogen-inoculated leaf to the distal organs, where salicylic acid-dependent defenses are activated. We demonstrate here that petiole exudates (PeXs) collected from Arabidopsis leaves inoculated with an avirulent (Avr) Pseudomonas syringae strain promote resistance when applied to Arabidopsis, tomato (Lycopersicum esculentum) and wheat (Triticum aestivum). Arabidopsis FATTY ACID DESATURASE7 (FAD7), SUPPRESSOR OF FATTY ACID DESATURASE DEFICIENCY1 (SFD1) and SFD2 genes are required for accumulation of the SAR-inducing activity. In contrast to Avr PeX from wild-type plants, Avr PeXs from fad7, sfd1 and sfd2 mutants were unable to activate SAR when applied to wild-type plants. However, the SAR-inducing activity was reconstituted by mixing Avr PeXs collected from fad7 and sfd1 with Avr PeX from the SAR-deficient dir1 mutant. Since FAD7, SFD1 and SFD2 are involved in plastid glycerolipid biosynthesis and SAR is also compromised in the Arabidopsis monogalactosyldiacylglycerol synthase1 mutant we suggest that a plastid glycerolipid-dependent factor is required in Avr PeX along with the DIR1-encoded lipid transfer protein for long-distance signaling in SAR. FAD7-synthesized lipids provide fatty acids for synthesis of jasmonic acid (JA). However, co-infiltration of JA and methylJA with Avr PeX from fad7 and sfd1 did not reconstitute the SAR-inducing activity. In addition, JA did not co-purify with the SAR-inducing activity confirming that JA is not the mobile signal in SAR.
Authors:
Ratnesh Chaturvedi; Kartikeya Krothapalli; Ragiba Makandar; Ashis Nandi; Alexis A Sparks; Mary R Roth; Ruth Welti; Jyoti Shah
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2007-12-15
Journal Detail:
Title:  The Plant journal : for cell and molecular biology     Volume:  54     ISSN:  1365-313X     ISO Abbreviation:  Plant J.     Publication Date:  2008 Apr 
Date Detail:
Created Date:  2008-03-20     Completed Date:  2008-05-07     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9207397     Medline TA:  Plant J     Country:  England    
Other Details:
Languages:  eng     Pagination:  106-17     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, University of North Texas, Denton, TX 76203, USA.
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MeSH Terms
Descriptor/Qualifier:
Arabidopsis / metabolism*
Arabidopsis Proteins / genetics,  metabolism
Carrier Proteins / genetics,  metabolism
Cyclopentanes / metabolism*
Fatty Acid Desaturases / genetics,  metabolism
Fatty Acids, Omega-3
Galactosyltransferases / genetics,  metabolism
Gene Expression Regulation, Plant
Glycerolphosphate Dehydrogenase / genetics,  metabolism
Mutation
Oxylipins / metabolism*
Plant Leaves / metabolism*
Plastids / metabolism*
Grant Support
ID/Acronym/Agency:
P20 RR016475/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Carrier Proteins; 0/Cyclopentanes; 0/Fatty Acids, Omega-3; 0/Oxylipins; 0/dir1-1 protein, Arabidopsis; 6894-38-8/jasmonic acid; EC 1.1.-/Glycerolphosphate Dehydrogenase; EC 1.1.1.94/SFD1 protein, Arabidopsis; EC 1.14.19.-/Fatty Acid Desaturases; EC 1.14.99.-/Fad7 protein, Arabidopsis; EC 1.14.99.-/SFD2 protein, Arabidopsis; EC 1.14.99.-/stearoyl ACP desaturase, Arabidopsis; EC 2.4.1.-/Galactosyltransferases; EC 2.4.1.46/1,2-diacylglycerol 3-beta-galactosyltransferase; EC 2.4.1.46/MGD1 protein, Arabidopsis

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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