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MBC in Press, published online ahead of print February 21, 2007
Mol. Biol. Cell 10.1091/mbc.E06-08-0718

A more recent version of this article appeared on April 1, 2007 Originally published as MBC in Press, 10.1091/mbc.E06-08-0718 on February 7, 2007
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Submitted on August 16, 2006
Revised on January 8, 2007
Accepted on January 31, 2007

Conserved Actin Cysteine Residues Are Oxidative Stress Sensors that Can Regulate Cell Death in Yeast

Michelle E. Farah and David C. Amberg

Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210

Monitoring Editor: Charles Boone

Actin’s functional complexity makes it a likely target of oxidative stress but also places it in a prime position to coordinate the response to oxidative stress. We have previously shown that the NADPH oxidoreductase Oye2p protects the actin cytoskeleton from oxidative stress. Here we demonstrate that the physiological consequence of actin oxidation is to accelerate cell death in yeast. Loss of Oye2p leads to ROS accumulation, activation of the oxidative stress response, nuclear fragmentation and DNA degradation and premature chronological aging of yeast cells. The oye2{Delta} phenotype can be completely suppressed by removing the potential for formation of the actin C285-C374 disulfide bond, the likely substrate of the Oye2p enzyme or by treating the cells with the clinically important reductant N-acetylcysteine. Because these two cysteines are coconserved in all actin isoforms, we theorize that we have uncovered a universal mechanism whereby actin helps to coordinate the cellular response to oxidative stress by both sensing and responding to oxidative load.

Address correspondence to: David C. Amberg (ambergd{at}upstate.edu)




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