Source:http://linkedlifedata.com/resource/pubmed/id/11169183
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
Salicylic acid (SA) plays a central role as a signalling molecule involved in plant defense against microbial attack. Genetic manipulation of SA biosynthesis may therefore help to generate plants that are more disease-resistant. By fusing the two bacterial genes pchA and pchB from Pseudomonas aeruginosa, which encode isochorismate synthase and isochorismate pyruvate-lyase, respectively, we have engineered a novel hybrid enzyme with salicylate synthase (SAS) activity. The pchB-A fusion was expressed in Arabidopsis thaliana under the control of the constitutive cauliflower mosaic virus (CaMV) 35S promoter, with targeting of the gene product either to the cytosol (c-SAS plants) or to the chloroplast (p-SAS plants). In p-SAS plants, the amount of free and conjugated SA was increased more than 20-fold above wild type (WT) level, indicating that SAS is functional in Arabidopsis. P-SAS plants showed a strongly dwarfed phenotype and produced very few seeds. Dwarfism could be caused by the high SA levels per se or, perhaps more likely, by a depletion of the chorismate or isochorismate pools of the chloroplast. Targeting of SAS to the cytosol caused a slight increase in free SA and a significant threefold increase in conjugated SA, probably reflecting limited chorismate availability in this compartment. Although this modest increase in total SA content did not strongly induce the resistance marker PR-1, it resulted nevertheless in enhanced disease resistance towards a virulent isolate of Peronospora parasitica. Increased resistance of c-SAS lines was paralleled with reduced seed production. Taken together, these results illustrate that SAS is a potent tool for the manipulation of SA levels in plants.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Codon,
http://linkedlifedata.com/resource/pubmed/chemical/Intramolecular Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Phenols,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Salicylates,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles,
http://linkedlifedata.com/resource/pubmed/chemical/isochorismate synthase,
http://linkedlifedata.com/resource/pubmed/chemical/pyochelin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0960-7412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
67-77
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11169183-Amino Acid Sequence,
pubmed-meshheading:11169183-Arabidopsis,
pubmed-meshheading:11169183-Base Sequence,
pubmed-meshheading:11169183-Caulimovirus,
pubmed-meshheading:11169183-Codon,
pubmed-meshheading:11169183-Intramolecular Transferases,
pubmed-meshheading:11169183-Lyases,
pubmed-meshheading:11169183-Molecular Sequence Data,
pubmed-meshheading:11169183-Phenols,
pubmed-meshheading:11169183-Plant Leaves,
pubmed-meshheading:11169183-Plants, Genetically Modified,
pubmed-meshheading:11169183-Pseudomonas aeruginosa,
pubmed-meshheading:11169183-Recombinant Fusion Proteins,
pubmed-meshheading:11169183-Restriction Mapping,
pubmed-meshheading:11169183-Salicylates,
pubmed-meshheading:11169183-Thiazoles
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pubmed:year |
2001
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pubmed:articleTitle |
Manipulation of salicylate content in Arabidopsis thaliana by the expression of an engineered bacterial salicylate synthase.
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pubmed:affiliation |
Département de Biologie, Université de Fribourg, CH-1700 Fribourg, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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