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J. Biol. Chem., Vol. 278, Issue 43, 41849-41855, October 24, 2003

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Lipid Hydroperoxides Activate the Mitogen-activated Protein Kinase Mpk1p in Saccharomyces cerevisiae^*

Nazif Alic, Vincent J. Higgins, Alena Pichova¶, Michael Breitenbach, and Ian W. Dawes||

From the Ramaciotti Centre for Gene Function Analysis and School of Biotechnology and Biomolecular Sciences, University of New South Wales, 2052 New South Wales, Australia, the Department of Genetics, University of Salzburg, Hellbrunnerstrasse 34, A-5020, Salzburg, Austria, and the ^¶Institute of Microbiology, Czech Academy of Sciences, Videnska 1083 Prague, Czech Republic

Saccharomyces cerevisiae is capable of responding to oxidants, including lipid peroxidation products. We investigate here the role of the mitogen-activated protein kinase Mpk1p in protection against linoleic acid hydroperoxide (LoaOOH), a product of radical attack on an unsaturated lipid. MPK1 was found to be required for resistance to LoaOOH. Furthermore, Mpk1p was rapidly and transiently phosphorylated in response to LoaOOH. This phosphorylation was dose-dependent and stimulated by sublethal concentrations as low as 1 µM in the external medium. Such low doses have been shown to result in resistance to subsequent challenge with a higher dose through the process of adaptation. However MPK1 was not essential for this adaptive response. MPK1 was also not involved in cell cycle modulation and acted independently of the cell cycle-regulating Oca1p. Transcriptional profiling of the mpk1 cells during LoaOOH stress indicated that Mpk1p may be important in effecting changes to the cell surface and metabolism during LoaOOH exposure. Furthermore, it revealed that Mpk1p is required for the regulation of 97 LoaOOH-responsive transcripts. Evidence is presented that the activation of Mpk1p may be caused by the activation of protein kinase C by LoaOOH.

Received for publication, July 17, 2003 , and in revised form, August 6, 2003.

^* This work was supported by grants from the Australian Research Council (to I. W. D.), by Grant No. P16402-B07 from the Austrian Fonds zur Forderung der Wissenschaftlichen Forschung (to M. B.), and by an Australian postgraduate award (to N.A.) 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.

The on-line version of this article (available at http://www.jbc.org) contains Supplementary Materials.

^|| To whom correspondence should be addressed. Tel.: 61-2-9385-2089; Fax: 61-2-9385-1050; E-mail: I.Dawes{at}unsw.edu.au.

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