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Originally published In Press as doi:10.1074/jbc.M307552200 on September 11, 2003

J. Biol. Chem., Vol. 278, Issue 48, 47905-47914, November 28, 2003
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Detoxification of the Fusarium Mycotoxin Deoxynivalenol by a UDP-glucosyltransferase from Arabidopsis thaliana*

Brigitte Poppenberger{ddagger}§, Franz Berthiller¶, Doris Lucyshyn{ddagger}, Tobias Sieberer{ddagger}, Rainer Schuhmacher¶, Rudolf Krska¶, Karl Kuchler||**, Josef Glössl{ddagger}, Christian Luschnig{ddagger}, and Gerhard Adam{ddagger}{ddagger}{ddagger}

From the {ddagger}Center of Applied Genetics, BOKU - University of Natural Resources and Applied Life Sciences, Muthgasse 18, A-1190 Vienna, Austria, the Center for Analytical Chemistry, Institute for Agrobiotechnology (IFA-Tulln), Konrad Lorenz Strasse 20, A-3430 Tulln, Austria, and the ||Department of Medical Biochemistry, Division of Molecular Genetics, Max F. Perutz Laboratories, University and BioCenter of Vienna, Dr. Bohrgasse 9/2, A-1030 Vienna, Austria

Plant pathogenic fungi of the genus Fusarium cause agriculturally important diseases of small grain cereals and maize. Trichothecenes are a class of mycotoxins produced by different Fusarium species that inhibit eukaryotic protein biosynthesis and presumably interfere with the expression of genes induced during the defense response of the plants. One of its members, deoxynivalenol, most likely acts as a virulence factor during fungal pathogenesis and frequently accumulates in grain to levels posing a threat to human and animal health. We report the isolation and characterization of a gene from Arabidopsis thaliana encoding a UDP-glycosyltransferase that is able to detoxify deoxynivalenol. The enzyme, previously assigned the identifier UGT73C5, catalyzes the transfer of glucose from UDP-glucose to the hydroxyl group at carbon 3 of deoxynivalenol. Using a wheat germ extract-coupled transcription/translation system we have shown that this enzymatic reaction inactivates the mycotoxin. This deoxynivalenol-glucosyltransferase (DOGT1) was also found to detoxify the acetylated derivative 15-acetyl-deoxynivalenol, whereas no protective activity was observed against the structurally similar nivalenol. Expression of the glucosyltransferase is developmentally regulated and induced by deoxynivalenol as well as salicylic acid, ethylene, and jasmonic acid. Constitutive overexpression in Arabidopsis leads to enhanced tolerance against deoxynivalenol.


Received for publication, July 14, 2003 , and in revised form, September 4, 2003.

* This work was supported by grants from the University of Natural Resources and Applied Life Sciences (BOKU Grant 600.032), the Federal Ministry for Education, Science and Culture (Austrian Genome Programme GEN-AU (Grant GZ 200.051/6-VI/1/2002)), and Scientific Collaboration with Iran (Grant GZ 309.007/3-VIII/B/8b/2000). 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.

§ Received a DOC fellowship from the Austrian Academy of Sciences.

** Supported by Austrian Science Foundation Grant P-15934-B08.

{ddagger}{ddagger} To whom correspondence should be addressed. Tel.: 43-1-36006-6380; Fax: 43-1-36006-6392; E-mail: gerhard.adam{at}boku.ac.at.


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