Budding yeast Saccharomyces cerevisiae as a model to study oxidative modification of proteins in eukaryotes

• Authors: Volodymyr I Lushchak
• Languages of publication: EN

Abstracts

EN

The budding yeast Saccharomyces cerevisiae is a well studied unicellular eukaryotic organism the genome of which has been sequenced. The use of yeast in many commercial systems makes its investigation important not only from basic, but also from practical point of view. Yeast may be grown under both aerobic and anaerobic conditions. The investigation of the response of eukaryotes to different kinds of stresses was pioneered owing to yeast and here we focus mainly on the so-called oxidative stress. It is a result of an imbalance between the formation and decomposition of reactive oxygen species increasing their steady-state concentration. Reactive oxygen species may attack any cellular component. In the present review oxidation of proteins in S. cerevisiae is analyzed. There are two connected approaches to study oxidative protein modification - characterization of the overall process and identification of individual oxidized proteins. Because all aerobic organisms possess special systems which defend them against reactive oxygen species, the involvement of so-called antioxidant enzymes, particularly superoxide dismutase and catalase, in the protection of proteins is also analyzed.

Keywords

EN

protein oxidation; Saccharomyces cerevisiae; reactive oxygen species; oxidative stress

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2006
• Volume: 53
• Issue: 4
• Pages: 679-684

Dates

published

2006

received

2006-06-06

revised

2006-08-08

accepted

2006-08-31

(unknown)

2006-10-26

Contributors

author

Volodymyr I Lushchak

• Department of Biochemistry, Vassyl Stefanyk Precarpathian National University, Ivano-Frankivsk, Ukraine

References

• Bagnyukova T, Vasylkiv O, Storey K, Lushchak V (2005) Catalase inhibition by amino triazole induces oxidative stress in goldfish brain. Brain Res 1052: 180-186.
• Bayliak MM, Semchyshyn HM, Lushchak VI (2006) Effect of hydrogen peroxide on antioxidant enzyme activities in Saccharomyces cerevisiae is strain-specific. Biochemistry (Moscow) 71: 1013-1020.
• Benov L, Fridovich I (1996) Functional significance of the Cu,ZnSOD in Escherichia coli. Arch Biochem Biophys 327: 249-253.
• Cabiscol E, Piulats E, Echave P, Herrero E, Ros J (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J Biol Chem 275: 27393-27398.
• Cabiscol E, Belli G, Tamarit J, Echave P, Herrero E, Ros J (2002) Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae. J Biol Chem 277: 44531-44538.
• Cocco D, Calabrese L, Rigo A, Argese E, Rotillio G (1981) Re-examination of the reaction of diethyldithiocarbamate with the copper of superoxide dismutase. J Biol Chem 256: 8983-8986.
• Gospodaryov D, Bayliak M, Lushchak V (2005) Free radical in vitro inactivation of glucose-6-phosphate dehydrogenase from the yeast Saccharomyces cerevisiae. Ukrainian Biochem J 77: 54-60.
• Halliwell B, Gutteridge JMC (1985) Free Radicals in Biology and Medicine. Clarendon, Oxford.
• Lenz A, Costabel U, Shaltiel S, Levine R (1989) Determination of carbonyl groups in oxidatively modified proteins by reduction with tritiated sodium borohydride. Anal Biochem 177: 419-425.
• Lushchak VI (2001) Oxidative stress and mechanisms of protection against it in bacteria. Biochemistry (Moscow) 66: 476-489.
• Lushchak VI (2002) Oxidative stress in bacteria. In Oxidative Stress at Molecular, Cellular and Organ Levels (Johnston P, Boldyrev AA eds) pp 45-65. Research Singpost, Trivandrum, India.
• Lushchak V, Gospodaryov D (2005) Catalases protect cellular proteins from oxidative modification in Saccharomyces cerevisiae. Cell Biol Int 29: 187-192.
• Lushchak V, Semchyshyn H, Mandryk S, Lushchak O (2005a) Possible role of superoxide dismutases in the yeast Saccharomyces cerevisiae under respiratory conditions. Arch Biochem Biophys 441: 35-40.
• Lushchak V, Semchyshyn H, Lushchak O, Mandryk S (2005b) Diethyldithiocarbamate inhibits in vivo Cu,Zn-superoxide dismutase and perturbs free radical processes in yeast Saccharomyces cerevisiae. Biochem Biophys Res Commun 338: 1739-1744.
• McCord J (1997) The importance of oxidant-antioxidant balance. In Oxidative Stress, Cancer, AIDS, and Neurodegenerative Diseases (Montagnier L, Olivier R, Pasquier C eds) pp 1-7. Marcel Dekker, New York.
• Mirzaei H, Regnier F (2006) Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrophotometry. Anal Chem 78: 770-778.
• O'Brien K, Dirmeier R, Engle M, Poyton R (2004) 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. J Biol Chem 279: 51817-51827.
• Reverter-Branchat G, Cabiscol E, Tamarit J, Ros J (2004) Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: common targets and prevention by calorie restriction. J Biol Chem 279: 31983-31989.
• Rodríguez-Manzaneque MT, Ros J, Cabiscol E, Sorribas A, Herrero E (1999) Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 19: 8180-8190.
• Rodríguez-Manzaneque MT, Tamarit J, Belli G, Ros J, Herrero E (2002) Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell 13: 1109-1121.
• Stadtman E (1993) Oxidation of free amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 62: 797-821.
• Stadtman E, Levine R (2000) Protein oxidation. Ann NY Acad Sci 899: 191-208.
• Yoo BS, Regnier FE (2004) Enrichment of carbonylated peptides using Girard P reagent and strong cation exchange chromatography. Electrophoresis 25: 1334-1341.