| pubmed-article:11169183 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11169183 | lifeskim:mentions | umls-concept:C0162740 | lld:lifeskim |
| pubmed-article:11169183 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:11169183 | lifeskim:mentions | umls-concept:C0947647 | lld:lifeskim |
| pubmed-article:11169183 | lifeskim:mentions | umls-concept:C0036075 | lld:lifeskim |
| pubmed-article:11169183 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:11169183 | lifeskim:mentions | umls-concept:C1550605 | lld:lifeskim |
| pubmed-article:11169183 | lifeskim:mentions | umls-concept:C0456205 | lld:lifeskim |
| pubmed-article:11169183 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:11169183 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:11169183 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:11169183 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
| pubmed-article:11169183 | 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. | lld:pubmed |
| pubmed-article:11169183 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11169183 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11169183 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11169183 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11169183 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11169183 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11169183 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11169183 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11169183 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11169183 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11169183 | pubmed:issn | 0960-7412 | lld:pubmed |
| pubmed-article:11169183 | pubmed:author | pubmed-author:MauckII | lld:pubmed |
| pubmed-article:11169183 | pubmed:author | pubmed-author:HaasDD | lld:pubmed |
| pubmed-article:11169183 | pubmed:author | pubmed-author:Mauch-ManiBB | lld:pubmed |
| pubmed-article:11169183 | pubmed:author | pubmed-author:KullBB | lld:pubmed |
| pubmed-article:11169183 | pubmed:author | pubmed-author:ReimmannCC | lld:pubmed |
| pubmed-article:11169183 | pubmed:author | pubmed-author:GailleCC | lld:pubmed |
| pubmed-article:11169183 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11169183 | pubmed:volume | 25 | lld:pubmed |
| pubmed-article:11169183 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11169183 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11169183 | pubmed:pagination | 67-77 | lld:pubmed |
| pubmed-article:11169183 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11169183 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11169183 | pubmed:articleTitle | Manipulation of salicylate content in Arabidopsis thaliana by the expression of an engineered bacterial salicylate synthase. | lld:pubmed |
| pubmed-article:11169183 | pubmed:affiliation | Département de Biologie, Université de Fribourg, CH-1700 Fribourg, Switzerland. | lld:pubmed |
| pubmed-article:11169183 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11169183 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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