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Applied and Environmental Microbiology, July 2006, p. 4885-4892, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.00526-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Old Yellow Enzymes Protect against Acrolein Toxicity in the Yeast Saccharomyces cerevisiae

Eleanor W. Trotter,1 Emma J. Collinson,1,{dagger} Ian W. Dawes,2 and Chris M. Grant1*

The University of Manchester, Faculty of Life Sciences, Manchester M13 9PT, United Kingdom,1 Ramaciotti Centre, School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW 2052, Australia2

Received 6 March 2006/ Accepted 16 May 2006

Acrolein is a ubiquitous reactive aldehyde which is formed as a product of lipid peroxidation in biological systems. In this present study, we screened the complete set of viable deletion strains in Saccharomyces cerevisiae for sensitivity to acrolein to identify cell functions involved in resistance to reactive aldehydes. We identified 128 mutants whose gene products are localized throughout the cell. Acrolein-sensitive mutants were distributed among most major biological processes but particularly affected gene expression, metabolism, and cellular signaling. Surprisingly, the screen did not identify any antioxidants or similar stress-protective molecules, indicating that acrolein toxicity may not be mediated via reactive oxygen species. Most strikingly, a mutant lacking an old yellow enzyme (OYE2) was identified as being acrolein sensitive. Old yellow enzymes are known to reduce {alpha},ß-unsaturated carbonyl compounds in vitro, but their physiological roles have remained uncertain. We show that mutants lacking OYE2, but not OYE3, are sensitive to acrolein, and overexpression of both isoenzymes increases acrolein tolerance. Our data indicate that OYE2 is required for basal levels of tolerance, whereas OYE3 expression is particularly induced following acrolein stress. Despite the range of {alpha},ß-unsaturated carbonyl compounds that have been identified as substrates of old yellow enzymes in vitro, we show that old yellow enzymes specifically mediate resistance to small {alpha},ß-unsaturated carbonyl compounds, such as acrolein, in vivo.

* Corresponding author. Mailing address: The University of Manchester, Faculty of Life Sciences, The Michael Smith Building, Oxford Road, Manchester M13 9PT, United Kingdom. Phone: (0161) 306 4192. Fax: (0161) 275 5082. E-mail: chris.grant{at}manchester.ac.uk.

{dagger} Present address: School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW 2052, Australia.

Applied and Environmental Microbiology, July 2006, p. 4885-4892, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.00526-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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  • Odat, O., Matta, S., Khalil, H., Kampranis, S. C., Pfau, R., Tsichlis, P. N., Makris, A. M. (2007). Old Yellow Enzymes, Highly Homologous FMN Oxidoreductases with Modulating Roles in Oxidative Stress and Programmed Cell Death in Yeast. J. Biol. Chem. 282: 36010-36023 [Abstract] [Full Text]  


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