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Overexpression of AtSGT1, an Arabidopsis salicylic acid glucosyltransferase, leads to increased susceptibility to Pseudomonas gringae

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dc.contributor.authorSong, Jong Tae-
dc.contributor.authorKoo, Yeon Jong-
dc.contributor.authorSeo, Hak Soo-
dc.contributor.authorKim, Min Chul-
dc.contributor.authorDo Choi, Yang-
dc.contributor.authorKim, Jeong Hoe-
dc.date.accessioned2022-12-27T06:11:38Z-
dc.date.available2022-12-27T06:11:38Z-
dc.date.issued2008-03-
dc.identifier.issn0031-9422-
dc.identifier.urihttps://scholarworks.gnu.ac.kr/handle/sw.gnu/27477-
dc.description.abstractWe reported previously that a recombinant salicylic acid (SA) glucosyltransferasel (AtSGT1) from Arabidopsis thaliana catalyzes the formation of both SA 2-O-beta-D-glucoside (SAG) and the glucose ester of SA (SGE). Here, transgenic Arabidopsis plants overexpressing AtSGT1 have been constructed, and their phenotypes analyzed. Compared to wild-type plants, transgenic plants showed an increased susceptibility to Pseudomonas syringae and reduced the accumulation levels of both free SA and its glucosylated forms (SAG and SGE). On the other hand, the overexpression increased the levels of methyl salicylate (MeSA) and methyl salicylate 2-O-beta-D-glucoside (MeSAG), and also induced SA carboxyl methyltransftrase1 (AtBSMT1) expression, whose products catalyze the conversion of SA to MeSA. Our data indicate that reduced resistance by AtSGT1 overexpression results from a reduction in SA content, which is at least in part caused by increases in MeSAG and MeSA levels at the expense of SA. Our study also suggests that genetic manipulation of AtSGT1 can be utilized as an important regulatory tool for pathogen control. (c) 2007 Elsevier Ltd. All rights reserved.-
dc.format.extent7-
dc.language영어-
dc.language.isoENG-
dc.publisherPERGAMON-ELSEVIER SCIENCE LTD-
dc.titleOverexpression of AtSGT1, an Arabidopsis salicylic acid glucosyltransferase, leads to increased susceptibility to Pseudomonas gringae-
dc.typeArticle-
dc.publisher.location영국-
dc.identifier.doi10.1016/j.phytochem.2007.12.010-
dc.identifier.scopusid2-s2.0-39549097308-
dc.identifier.wosid000254765200004-
dc.identifier.bibliographicCitationPHYTOCHEMISTRY, v.69, no.5, pp 1128 - 1134-
dc.citation.titlePHYTOCHEMISTRY-
dc.citation.volume69-
dc.citation.number5-
dc.citation.startPage1128-
dc.citation.endPage1134-
dc.type.docTypeArticle-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaPlant Sciences-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryPlant Sciences-
dc.subject.keywordPlusMETHYL SALICYLATE-
dc.subject.keywordPlusTOBACCO-
dc.subject.keywordPlusGLYCOSYLTRANSFERASES-
dc.subject.keywordPlusGLUCOSYLATION-
dc.subject.keywordPlusBIOSYNTHESIS-
dc.subject.keywordPlusLOCALIZATION-
dc.subject.keywordPlusCONJUGATION-
dc.subject.keywordPlusMETABOLISM-
dc.subject.keywordPlusINDUCTION-
dc.subject.keywordPlusGLUCOSE-
dc.subject.keywordAuthorArabidopsis thaliana-
dc.subject.keywordAuthorplant disease resistance-
dc.subject.keywordAuthorsalicylic acid (SA)-
dc.subject.keywordAuthorSA glucosyltransferase-
dc.subject.keywordAuthorSA conjugate-
dc.subject.keywordAuthorSA metabolite-
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