Source:http://linkedlifedata.com/resource/pubmed/id/19036031
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
2009-3-18
|
| pubmed:abstractText |
Salicylic acid (SA) is an important regulator of plant resistance to biotrophic and hemi-biotrophic pathogens. The enhanced pseudomonas susceptibility 1 (eps1) mutant in Arabidopsis thaliana is hypersusceptible to both virulent and avirulent strains of the bacterial pathogen Pseudomonas syringae. Through positional cloning, the EPS1 gene was isolated and found to encode a novel member of the BAHD acyltransferase superfamily. Pathogen-induced accumulation of SA and expression of pathogenesis-related (PR) genes were compromised in the eps1 mutant. SA could induce PR1 gene expression and restore disease resistance in the eps1 mutant. These results suggest that EPS1 functions upstream of SA and may be involved directly in synthesis of a precursor or a regulatory molecule for SA biosynthesis. Mutations of EPS1 or other genes important for SA accumulation or signaling conferred enhanced resistance to the necrotrophic fungal pathogens Botrytis cinerea and Alternaria brassicicola in the Nossen-0 background but had little effect in the Columbia-0 background. These results suggest that there is natural variation among Arabidopsis ecotypes with respect to the antagonistic cross-talk between defense signaling pathways against various types of microbial pathogens.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Salicylic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/T-DNA,
http://linkedlifedata.com/resource/pubmed/chemical/pathogenesis-related proteins, plant
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
1365-313X
|
| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:volume |
57
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1040-53
|
| pubmed:meshHeading |
pubmed-meshheading:19036031-Alternaria,
pubmed-meshheading:19036031-Amino Acid Sequence,
pubmed-meshheading:19036031-Arabidopsis,
pubmed-meshheading:19036031-Arabidopsis Proteins,
pubmed-meshheading:19036031-Botrytis,
pubmed-meshheading:19036031-Chromosome Mapping,
pubmed-meshheading:19036031-Cloning, Molecular,
pubmed-meshheading:19036031-DNA, Bacterial,
pubmed-meshheading:19036031-DNA, Plant,
pubmed-meshheading:19036031-Genes, Plant,
pubmed-meshheading:19036031-Genetic Complementation Test,
pubmed-meshheading:19036031-Immunity, Innate,
pubmed-meshheading:19036031-Molecular Sequence Data,
pubmed-meshheading:19036031-Mutagenesis, Insertional,
pubmed-meshheading:19036031-Mutation,
pubmed-meshheading:19036031-Plant Diseases,
pubmed-meshheading:19036031-Plant Proteins,
pubmed-meshheading:19036031-Pseudomonas syringae,
pubmed-meshheading:19036031-Salicylic Acid
|
| pubmed:year |
2009
|
| pubmed:articleTitle |
An important role of a BAHD acyl transferase-like protein in plant innate immunity.
|
| pubmed:affiliation |
Department of Botany and Plant Pathology, 915 W. State Street, Purdue University, West Lafayette, IN 47907-2054, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
|