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J. Biol. Chem., Vol. 279, Issue 50, 51817-51827, December 10, 2004

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Mitochondrial Protein Oxidation in Yeast Mutants Lacking Manganese-(MnSOD) or Copper- and Zinc-containing Superoxide Dismutase (CuZnSOD)

EVIDENCE THAT MnSOD AND CuZnSOD HAVE BOTH UNIQUE AND OVERLAPPING FUNCTIONS IN PROTECTING MITOCHONDRIAL PROTEINS FROM OXIDATIVE DAMAGE^*

Kristin M. O'Brien, Reinhard Dirmeier, Marcella Engle, and Robert O. Poyton

From the Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347

Saccharomyces cerevisiae expresses two forms of superoxide dismutase (SOD): MnSOD, encoded by SOD2, which is located within the mitochondrial matrix, and CuZnSOD, encoded by SOD1, which is located in both the cytosol and the mitochondrial intermembrane space. Because two different SOD enzymes are located in the mitochondrion, we examined the relative roles of each in protecting mitochondria against oxidative stress. Using protein carbonylation as a measure of oxidative stress, we have found no correlation between overall levels of respiration and the level of oxidative mitochondrial protein damage in either wild type or sod mutant strains. Moreover, mitochondrial protein carbonylation levels in sod1, sod2, and sod1sod2 mutants are not elevated in cells harvested from mid-logarithmic and early stationary phases, suggesting that neither MnSOD nor CuZnSOD is required for protecting the majority of mitochondrial proteins from oxidative damage during these early phases of growth. During late stationary phase, mitochondrial protein carbonylation increases in all strains, particularly in sod1 and sod1sod2 mutants. By using matrix-assisted laser desorption ionization time-of-flight mass spectrometry, we have found that specific proteins become carbonylated in sod1 and sod2 mutants. We identified six mitochondrial protein spots representing five unique proteins that become carbonylated in a sod1 mutant and 19 mitochondrial protein spots representing 11 unique proteins that become carbonylated in a sod2 mutant. Although some of the same proteins are carbonylated in both mutants, other proteins are not. These findings indicate that MnSOD and CuZnSOD have both unique and overlapping functions in the mitochondrion.

Received for publication, May 27, 2004 , and in revised form, September 21, 2004.

^* This work supported by National Institutes of Health Grant GM30228 (to R. O. P), and a National Institutes of Health National Research Service Award postdoctoral fellowship (to K. M. O.). 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.

Present address: Inst. of Arctic Biology, University of Alaska, Fairbanks, AK 99775-7000.

To whom correspondence should be addressed. Tel.: 303-493-3823; Fax: 303-492-3883; E-mail: Poyton{at}spot.colorado.edu.

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