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Vol. 15, Issue 5, 2049-2060, May 2004

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Transcriptional Activation of Metalloid Tolerance Genes in Saccharomyces cerevisiae Requires the AP-1–like Proteins Yap1p and Yap8p

Robert Wysocki ^*  , Pierre-Karl Fortier ^* , Ewa Maciaszczyk , Michael Thorsen ^||, Anick Leduc , Åsa Odhagen ^||, Grzegorz Owsianik ^¶, Stanislaw Ulaszewski , Dindial Ramotar , and Markus J. Tamás ^|| @

Institute of Genetics and Microbiology, Wroclaw University, 51-148 Wroclaw, Poland; Guy-Bernier Research Centre, University of Montreal, Montreal, Quebec, Canada H1T 2M4; ^|| Department of Cell and Molecular Biology/Microbiology, Göteborg University, S-405 30 Göteborg, Sweden; and ^¶ Unité de Biochimie Physiologique, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium

Submitted April 16, 2003; Revised December 23, 2003; Accepted January 21, 2004
Monitoring Editor: Pamela Silver

All organisms are equipped with systems for detoxification of the metalloids arsenic and antimony. Here, we show that two parallel pathways involving the AP-1–like proteins Yap1p and Yap8p are required for acquisition of metalloid tolerance in the budding yeast S. cerevisiae. Yap8p is demonstrated to reside in the nucleus where it mediates enhanced expression of the arsenic detoxification genes ACR2 and ACR3. Using chromatin immunoprecipitation assays, we show that Yap8p is associated with the ACR3 promoter in untreated as well as arsenic-exposed cells. Like for Yap1p, specific cysteine residues are critical for Yap8p function. We further show that metalloid exposure triggers nuclear accumulation of Yap1p and stimulates expression of antioxidant genes. Yap1p mutants that are unable to accumulate in the nucleus during H₂O₂ treatment showed nearly normal nuclear retention in response to metalloid exposure. Thus, our data are the first to demonstrate that Yap1p is being regulated by metalloid stress and to indicate that this activation of Yap1p operates in a manner distinct from stress caused by chemical oxidants. We conclude that Yap1p and Yap8p mediate tolerance by controlling separate subsets of detoxification genes and propose that the two AP-1–like proteins respond to metalloids through distinct mechanisms.

^* These authors contributed equally to this work.

Present addresses: Center for Molecular Oncology, University of Chicago, Chicago, IL 60637; Laboratorium voor Fysiologie, Katholieke Universiteit Leuven, Herestraat 49, B-3000 Leuven, Belgium.

^@ Corresponding author. E-mail address: markus.tamas{at}gmm.gu.se.

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