Differential cysteine depletion in respiratory chain complexes enables the distinction of longevity from aerobicity

Mechanisms of Ageing and Development

Volumn 132, Issue 4, 2011, Pages 171-179

  Schindeldecker, Mario ^a   Stark, Marcel ^a   Behl, Christian ^a   Moosmann, Bernd ^a  

^a UNIVERSITY MEDICAL CENTER MAINZ   (Germany)

Author keywords

Lifespan; Mitochondria; Oxidative stress; Protein oxidation; Respiration

Indexed keywords

COMPLEX V; CYSTEINE; CYTOCHROME C OXIDASE; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; RADICAL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG;

AEROBIC METABOLISM; ARTICLE; CELL NUCLEUS; CONTROLLED STUDY; HYDROPHOBICITY; LIFESPAN; LONGEVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEFECT; PROTEIN DEPLETION; PROTEIN DOMAIN; RESPIRATORY CHAIN;

AEROBIOSIS; AGING; ANIMALS; CELL NUCLEUS; CYSTEINE; ELECTRON TRANSPORT; HUMANS; MEMBRANE PROTEINS; MITOCHONDRIA; OXIDATIVE STRESS; OXYGEN CONSUMPTION; PHYLOGENY; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SULFHYDRYL COMPOUNDS; TIME FACTORS;

ANIMALIA;

EID: 79955782703     PISSN: 00476374     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mad.2011.03.002     Document Type: Article

References (28)

1. Bender A., Hajieva P., Moosmann B. Adaptive antioxidant methionine accumulation in respiratory chain complexes explains the use of a deviant genetic code in mitochondria. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:16496-16501.
2. Bernsel A., Viklund H., Hennerdal A., Elofsson A. TOPCONS: consensus prediction of membrane protein topology. Nucleic Acids Res. 2009, 37:W465-W468.
3. Brand M.D. The sites and topology of mitochondrial superoxide production. Exp. Gerontol. 2010, 45:466-472.
4. Davies M.J., Fu S., Wang H., Dean R.T. Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Radic. Biol. Med. 1999, 27:1151-1163.
5. Garland T., Harvey P.H., Ives A.R. Procedures for the analysis of comparative data using phylogenetically independent contrasts. Syst. Biol. 1992, 41:18-32.
6. Giles G.I., Jacob C. Reactive sulfur species: an emerging concept in oxidative stress. Biol. Chem. 2002, 383:375-388.
7. Hawkins C.L., Davies M.J. Generation and propagation of radical reactions on proteins. Biochim. Biophys. Acta 2001, 1504:196-219.
8. Heller H., Schaefer M., Schulten K. Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid crystal phase. J. Phys. Chem. 1993, 97:8343-8360.
9. Imlay J.A. Pathways of oxidative damage. Annu. Rev. Microbiol. 2003, 57:395-418.
10. Krogh A., Larsson B., von Heijne G., Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305:567-580.
11. Lenaz G., Genova M.L. Structural and functional organization of the mitochondrial respiratory chain: a dynamic super-assembly. Int. J. Biochem. Cell Biol. 2009, 41:1750-1772.
12. Levine R.L. Carbonyl modified proteins in cellular regulation, aging, and disease. Free Radic. Biol. Med. 2002, 32:790-796.
13. Levine R.L., Mosoni L., Berlett B.S., Stadtman E.R. Methionine residues as endogenous antioxidants in proteins. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:15036-15040.
14. Luo S., Levine R.L. Methionine in proteins defends against oxidative stress. FASEB J. 2009, 23:464-472.
15. Moosmann B., Behl C. Cytoprotective antioxidant function of tyrosine and tryptophan residues in transmembrane proteins. Eur. J. Biochem. 2000, 267:5687-5692.
16. Moosmann B., Behl C. Mitochondrially encoded cysteine predicts animal lifespan. Aging Cell 2008, 7:32-46.
17. Moosmann B. Respiratory chain cysteine and methionine usage indicate a causal role for thiyl radicals in aging. Exp. Gerontol. 2011, 46:164-169.
18. Muramoto K., Ohta K., Shinzawa-Itoh K., Kanda K., Taniguchi M., Nabekura H., Yamashita E., Tsukihara T., Yoshikawa S. Bovine cytochrome c oxidase structures enable O2 reduction with minimization of reactive oxygens and provide a proton-pumping gate. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:7740-7745.
19. Page M.M., Richardson J., Wiens B.E., Tiedtke E., Peters C.W., Faure P.A., Burness G., Stuart J.A. Antioxidant enzyme activities are not broadly correlated with longevity in 14 vertebrate endotherm species. Age 2010, 32:255-270.
20. Pamplona R., Barja G. Highly resistant macromolecular components and low rate of generation of endogenous damage: two key traits of longevity. Ageing Res. Rev. 2007, 6:189-210.
21. Popot J.L., de Vitry C. On the microassembly of integral membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 1990, 19:369-403.
22. Pryor W.A. Oxy-radicals and related species: their formation, lifetimes, and reactions. Annu. Rev. Physiol. 1986, 48:657-667.
23. Saran M., Bors W. Signalling by O2- and NO.: how far can either radical, or any specific reaction product, transmit a message under in vivo conditions? Chem. Biol. Interact. 1994, 90:35-45.
24. Schagger H., Pfeiffer K. The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes. J. Biol. Chem. 2001, 276:37861-37867.
25. Schwerzmann K., Cruz-Orive L.M., Eggman R., Sanger A., Weibel E.R. Molecular architecture of the inner membrane of mitochondria from rat liver: a combined biochemical and stereological study. J. Cell Biol. 1986, 102:97-103.
26. Stajich J.E., Block D., Boulez K., Brenner S.E., Chervitz S.A., Dagdigian C., Fuellen G., Gilbert J.G., Korf I., Lapp H., Lehvaslaiho H., Matsalla C., Mungall C.J., Osborne B.I., Pocock M.R., Schattner P., Senger M., Stein L.D., Stupka E., Wilkinson M.D., Birney E. The Bioperl toolkit: perl modules for the life sciences. Genome Res. 2002, 12:1611-1618.
27. Vieira-Silva S., Rocha E.P. An assessment of the impacts of molecular oxygen on the evolution of proteomes. Mol. Biol. Evol. 2008, 25:1931-1942.
28. Vogt W. Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic. Biol. Med. 1995, 18:93-105.