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J. Biol. Chem., Vol. 279, Issue 49, 50717-50725, December 3, 2004

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Desulfoglucosinolate Sulfotransferases from Arabidopsis thaliana Catalyze the Final Step in the Biosynthesis of the Glucosinolate Core Structure^*

Markus Piotrowski, Andreas Schemenewitz, Anna Lopukhina, Axel Müller, Tim Janowitz, Elmar W. Weiler, and Claudia Oecking¶

From the Department of Plant Physiology, Ruhr-Universität, Universitätsstrasse 150, 44801 Bochum, Germany and ^¶Plant Physiology, Center for Plant Molecular Biology, University of Tübingen, Auf der Morgenstelle 5, 72076 Tübingen, Germany

The phytotoxin coronatine is a structural analog of octadecanoid signaling molecules, which are well known mediators of plant defense reactions. To isolate novel coronatine-regulated genes from Arabidopsis thaliana, differential mRNA display was performed. Transcript levels of CORI-7 (coronatine induced-7) were rapidly and transiently increased in coronatine-treated plants, and the corresponding cDNA was found to encode the sulfotransferase AtST5a. Likewise, upon wounding, an immediate and transient increase in AtST5a mRNA levels could be observed in both locally wounded and unwounded (systemic) leaves. Furthermore, application of octadecanoids and ethylene as compounds involved in plant wound defense reactions resulted in AtST5a gene activation, whereas pathogen defense-related signals (yeast elicitor and salicylic acid) were inactive. AtST5a and its close homologs AtST5b and AtST5c were purified as His₆ -tagged proteins from Escherichia coli. The three enzymes were shown to catalyze the final step in the biosynthesis of the glucosinolate (GS) core structure, the sulfation of desulfoglucosinolates (dsGSs). They accept a broad range of dsGSs as substrates. However, in a competitive situation, AtST5a clearly prefers tryptophan- and phenylalanine-derived dsGSs, whereas long chain dsGSs derived from methionine are the preferred substrates of AtST5b and AtST5c. Treatment of Arabidopsis plants with low concentrations of coronatine resulted in an increase in the amounts of specific GSs, primarily glucobrassicin and neoglucobrassicin. Hence, it is suggested that AtST5a is the sulfotransferase responsible for the biosynthesis of tryptophan-derived GSs in vivo.

Received for publication, July 8, 2004 , and in revised form, September 3, 2004.

^* This work was supported in part by Deutsche Forschungsgemein-schaft Grants SPP1152 (to M. P.) and SFB446-A18 (to C. O.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 49-234-322-4291; Fax: 49-234-321-4187; E-mail: Elmar.Weiler{at}ruhr-unibochum.de.

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