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Applied and Environmental Microbiology, June 2006, p. 4404-4410, Vol. 72, No. 6
0099-2240/06/$08.00+0 doi:10.1128/AEM.02544-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Heterologous Expression of Arabidopsis UDP-Glucosyltransferases in Saccharomyces cerevisiae for Production of Zearalenone-4-O-Glucoside
Brigitte Poppenberger,1,
Franz Berthiller,2
Herwig Bachmann,1,
Doris Lucyshyn,1
Clemens Peterbauer,1,
Rudolf Mitterbauer,1
Rainer Schuhmacher,2
Rudolf Krska,2
Josef Glössl,1 and
Gerhard Adam1*
Institute of Applied Genetics and Cell Biology, Department of Applied Plant Sciences and Plant Biotechnology, BOKU—University of Natural Resources and Applied Life Sciences, Muthgasse 18, A-1190 Vienna, Austria,1 Center for Analytical Chemistry and Christian Doppler Laboratory for Mycotoxin Research, Department of Agrobiotechnology-IFA Tulln, BOKU—University of Natural Resources and Applied Life Sciences, Konrad Lorenz Strasse 20, A-3430 Tulln, Austria2
Received 28 October 2005/ Accepted 4 April 2006
Zearalenone, a secondary metabolite produced by several plant-pathogenic fungi of the genus Fusarium, has high estrogenic activity in vertebrates. We developed a Saccharomyces cerevisiae bioassay strain that we used to identify plant genes encoding UDP-glucosyltransferases that can convert zearalenone into zearalenone-4-O-glucoside (ZON-4-O-Glc). Attachment of the glucose moiety to zearalenone prevented the interaction of the mycotoxin with the human estrogen receptor. We found that two of six clustered, similar UGT73C genes of Arabidopsis thaliana encode glucosyltransferases that can inactivate zearalenone in the yeast bioassay. The formation of glucose conjugates seems to be an important plant mechanism for coping with zearalenone but may result in significant amounts of "masked" zearalenone in Fusarium-infected plant products. Due to the unavailability of an analytical standard, the ZON-4-O-Glc is not measured in routine analytical procedures, even though it can be converted back to active zearalenone in the digestive tracts of animals. Zearalenone added to yeast transformed with UGT73C6 was converted rapidly and efficiently to ZON-4-O-Glc, suggesting that the cloned UDP-glucosyltransferase could be used to produce reference glucosides of zearalenone and its derivatives.
* Corresponding author. Mailing address: Institute of Applied Genetics and Cell Biology, Department of Applied Plant Sciences and Plant Biotechnology, BOKU—University of Natural Resources and Applied Life Sciences, Muthgasse 18, A-1190 Vienna, Austria. Phone: 0043-1-36006 6380. Fax: 0043-1-36006 6392. E-mail: gerhard.adam{at}boku.ac.at.
Present address: CNAP, Department of Biology, University of York, YO10 5DD York, United Kingdom.
Present address: NIZO Food Research, Kernhemseweg 2, P.O. Box 20, 6710 BA Ede, The Netherlands.
Present address: Division of Food Biotechnology, Department of Food Sciences and Technology, BOKU—University of Natural Resources and Applied Life Sciences Vienna, Muthgasse 18, A-1190 Vienna, Austria.
Applied and Environmental Microbiology, June 2006, p. 4404-4410, Vol. 72, No. 6
0099-2240/06/$08.00+0 doi:10.1128/AEM.02544-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
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