Document Detail


Biochemical and molecular characterization of a hydroxyjasmonate sulfotransferase from Arabidopsis thaliana.
MedLine Citation:
PMID:  12637544     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
12-Hydroxyjasmonate, also known as tuberonic acid, was first isolated from Solanum tuberosum and was shown to have tuber-inducing properties. It is derived from the ubiquitously occurring jasmonic acid, an important signaling molecule mediating diverse developmental processes and plant defense responses. We report here that the gene AtST2a from Arabidopsis thaliana encodes a hydroxyjasmonate sulfotransferase. The recombinant AtST2a protein was found to exhibit strict specificity for 11- and 12-hydroxyjasmonate with K(m) values of 50 and 10 microm, respectively. Furthermore, 12-hydroxyjasmonate and its sulfonated derivative are shown to be naturally occurring in A. thaliana. The exogenous application of methyljasmonate to A. thaliana plants led to increased levels of both metabolites, whereas treatment with 12-hydroxyjasmonate led to increased level of 12-hydroxyjasmonate sulfate without affecting the endogenous level of jasmonic acid. AtST2a expression was found to be induced following treatment with methyljasmonate and 12-hydroxyjasmonate. In contrast, the expression of the methyljasmonate-responsive gene Thi2.1, a marker gene in plant defense responses, is not induced upon treatment with 12-hydroxyjasmonate indicating the existence of independent signaling pathways responding to jasmonic acid and 12-hydroxyjasmonic acid. Taken together, the results suggest that the hydroxylation and sulfonation reactions might be components of a pathway that inactivates excess jasmonic acid in plants. Alternatively, the function of AtST2a might be to control the biological activity of 12-hydroxyjasmonic acid.
Authors:
Satinder Kaur Gidda; Otto Miersch; Anastasia Levitin; Jurgen Schmidt; Claus Wasternack; Luc Varin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2003-03-10
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  278     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2003 May 
Date Detail:
Created Date:  2003-05-12     Completed Date:  2003-06-25     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  17895-900     Citation Subset:  IM    
Affiliation:
Center for Structural and Functional Genomics, Biology Department, Concordia University, Montreal H3G 1M8, Canada.
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MeSH Terms
Descriptor/Qualifier:
Acetic Acids / chemistry,  metabolism
Amino Acid Sequence
Arabidopsis / enzymology*
Arabidopsis Proteins / chemistry*,  genetics*
Blotting, Northern
Chromatography, Liquid
Cloning, Molecular
Cyclopentanes / chemistry,  metabolism
Electrophoresis, Polyacrylamide Gel
Kinetics
Mass Spectrometry
Molecular Sequence Data
Oxylipins
Plants, Genetically Modified
RNA, Messenger / metabolism
Recombinant Proteins / metabolism
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
Sulfotransferases / chemistry*,  genetics*
Chemical
Reg. No./Substance:
0/Acetic Acids; 0/Arabidopsis Proteins; 0/Cyclopentanes; 0/Oxylipins; 0/RNA, Messenger; 0/Recombinant Proteins; 1211-29-6/methyl jasmonate; 6894-38-8/jasmonic acid; EC 2.8.2.-/Sulfotransferases; EC 2.8.2.-/hydroxyjasmonate sulfotransferase, Arabidopsis

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


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