메뉴 건너뛰기




Volumn 105, Issue 43, 2008, Pages 16496-16501

Adaptive antioxidant methionine accumulation in respiratory chain complexes explains the use of a deviant genetic code in mitochondria

Author keywords

Evolution; Methionine sulfoxide; Nonstandard genetic code; Oxidative stress; Protein oxidation

Indexed keywords

ANTIOXIDANT; CYTOCHROME B; ISOLEUCINE; METHIONINE; PROTEOME; REACTIVE OXYGEN METABOLITE;

EID: 55949132715     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0802779105     Document Type: Article
Times cited : (93)

References (42)
  • 1
    • 0018577407 scopus 로고
    • A different genetic code in human mitochondria
    • Barrell BG, Bankier AT, Drouin J (1979) A different genetic code in human mitochondria. Nature 282:189-194.
    • (1979) Nature , vol.282 , pp. 189-194
    • Barrell, B.G.1    Bankier, A.T.2    Drouin, J.3
  • 2
    • 0035234558 scopus 로고    scopus 로고
    • Rewiring the keyboard: Evolvability of the genetic code
    • Knight RD, Freeland SJ, Landweber LF (2001) Rewiring the keyboard: Evolvability of the genetic code. Nat Rev Genet 2:49-58.
    • (2001) Nat Rev Genet , vol.2 , pp. 49-58
    • Knight, R.D.1    Freeland, S.J.2    Landweber, L.F.3
  • 3
    • 1642513699 scopus 로고    scopus 로고
    • Driving change: The evolution of alternative genetic codes
    • Santos MA, Moura G, Massey SE, Tuite MF (2004) Driving change: The evolution of alternative genetic codes. Trends Genet 20:95-102.
    • (2004) Trends Genet , vol.20 , pp. 95-102
    • Santos, M.A.1    Moura, G.2    Massey, S.E.3    Tuite, M.F.4
  • 4
    • 0026574207 scopus 로고
    • Recent evidence for evolution of the genetic code
    • Osawa S, Jukes TH, Watanabe K, Muto A (1992) Recent evidence for evolution of the genetic code. Microbiol Rev 56:229-264.
    • (1992) Microbiol Rev , vol.56 , pp. 229-264
    • Osawa, S.1    Jukes, T.H.2    Watanabe, K.3    Muto, A.4
  • 5
    • 0014378880 scopus 로고
    • The origin of the genetic code
    • Crick FH (1968) The origin of the genetic code. J Mol Biol 38:367-379.
    • (1968) J Mol Biol , vol.38 , pp. 367-379
    • Crick, F.H.1
  • 6
    • 2942537836 scopus 로고    scopus 로고
    • Artificially ambiguous genetic code confers growth yield advantage
    • Pezo V, et al. (2004) Artificially ambiguous genetic code confers growth yield advantage. Proc Natl Acad Sci USA 101:8593-9597.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8593-9597
    • Pezo, V.1
  • 7
    • 0030138792 scopus 로고    scopus 로고
    • On malleability in the genetic code
    • Schultz DW, Yarus M (1996) On malleability in the genetic code. J Mol Evol 42:597-601.
    • (1996) J Mol Evol , vol.42 , pp. 597-601
    • Schultz, D.W.1    Yarus, M.2
  • 8
    • 14644437032 scopus 로고    scopus 로고
    • Mitochondrial genetic codes evolve to match amino acid requirements of proteins
    • Swire J, Judson OP, Burt A (2005) Mitochondrial genetic codes evolve to match amino acid requirements of proteins. J Mol Evol 60:128-139.
    • (2005) J Mol Evol , vol.60 , pp. 128-139
    • Swire, J.1    Judson, O.P.2    Burt, A.3
  • 9
    • 34250704167 scopus 로고    scopus 로고
    • The mechanisms of codon reassignments in mitochondrial genetic codes
    • Sengupta S, Yang X, Higgs PG (2007) The mechanisms of codon reassignments in mitochondrial genetic codes. J Mol Evol 64:662-688.
    • (2007) J Mol Evol , vol.64 , pp. 662-688
    • Sengupta, S.1    Yang, X.2    Higgs, P.G.3
  • 10
    • 0031180638 scopus 로고    scopus 로고
    • Further comments on codon reassignment
    • Jukes TH, Osawa S (1997) Further comments on codon reassignment. J Mol Evol 45:1-3.
    • (1997) J Mol Evol , vol.45 , pp. 1-3
    • Jukes, T.H.1    Osawa, S.2
  • 11
    • 0031182554 scopus 로고    scopus 로고
    • Further comments on codon reassignment. Response
    • Yarus M, Schultz DW (1997) Further comments on codon reassignment. Response. J Mol Evol 45:3-6.
    • (1997) J Mol Evol , vol.45 , pp. 3-6
    • Yarus, M.1    Schultz, D.W.2
  • 12
    • 0032584155 scopus 로고    scopus 로고
    • Codon reassignment and amino acid composition in hemichordate mitochondria
    • Castresana J, Feldmaier-Fuchs G, Pääbo S (1998) Codon reassignment and amino acid composition in hemichordate mitochondria. Proc Natl Acad Sci USA 95:3703-3707.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3703-3707
    • Castresana, J.1    Feldmaier-Fuchs, G.2    Pääbo, S.3
  • 13
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt W (1995) Oxidation of methionyl residues in proteins: Tools, targets, and reversal. Free Radic Biol Med 18:93-105.
    • (1995) Free Radic Biol Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 14
    • 0037082129 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase: Structure, mechanism of action, and biological function
    • Weissbach H, et al. (2002) Peptide methionine sulfoxide reductase: Structure, mechanism of action, and biological function. Arch Biochem Biophys 397:172-178.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 172-178
    • Weissbach, H.1
  • 15
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • Moskovitz J (2005) Methionine sulfoxide reductases: Ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Biochim Biophys Acta 1703:213-219.
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 213-219
    • Moskovitz, J.1
  • 16
    • 0035818520 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals
    • Moskovitz J, et al. (2001) Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci USA 98:12920-12925.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12920-12925
    • Moskovitz, J.1
  • 17
    • 4244218956 scopus 로고    scopus 로고
    • Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism
    • 235
    • Stadtman ER, Moskovitz J, Berlett BS, Levine RL (2002) Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism. Mol Cell Biochem 234- 235:3-9.
    • (2002) Mol Cell Biochem , vol.234 , pp. 3-9
    • Stadtman, E.R.1    Moskovitz, J.2    Berlett, B.S.3    Levine, R.L.4
  • 18
    • 33748680912 scopus 로고    scopus 로고
    • Silencing of the methionine sulfoxide reductase A gene results in loss of mitochondrial membrane potential and increased ROS production in human lens cells
    • Marchetti MA, et al. (2006) Silencing of the methionine sulfoxide reductase A gene results in loss of mitochondrial membrane potential and increased ROS production in human lens cells. Exp Eye Res 83:1281-1286.
    • (2006) Exp Eye Res , vol.83 , pp. 1281-1286
    • Marchetti, M.A.1
  • 20
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas E, Davies KJ (2000) Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 29:222-230.
    • (2000) Free Radic Biol Med , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 22
    • 0032924757 scopus 로고    scopus 로고
    • Mitochondrial damage induced by conditions of oxidative stress
    • Kowaltowski AJ, Vercesi AE (1999) Mitochondrial damage induced by conditions of oxidative stress. Free Radic Biol Med 26:463-471.
    • (1999) Free Radic Biol Med , vol.26 , pp. 463-471
    • Kowaltowski, A.J.1    Vercesi, A.E.2
  • 23
    • 0035917814 scopus 로고    scopus 로고
    • Mitochondrial permeability transition and oxidative stress
    • Kowaltowski AJ, Castilho RF, Vercesi AE (2001) Mitochondrial permeability transition and oxidative stress. FEBS Lett 495:12-15.
    • (2001) FEBS Lett , vol.495 , pp. 12-15
    • Kowaltowski, A.J.1    Castilho, R.F.2    Vercesi, A.E.3
  • 24
    • 38349126762 scopus 로고    scopus 로고
    • Mitochondrially encoded cysteine predicts animal lifespan
    • Moosmann B, Behl C (2008) Mitochondrially encoded cysteine predicts animal lifespan. Aging Cell 7:32-46.
    • (2008) Aging Cell , vol.7 , pp. 32-46
    • Moosmann, B.1    Behl, C.2
  • 26
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D (1994) Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77:817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 27
    • 34548148201 scopus 로고    scopus 로고
    • Hydrogen peroxide: A metabolic by-product or a common mediator of ageing signals?
    • Giorgio M, Trinei M, Migliaccio E, Pelicci PG (2007) Hydrogen peroxide: A metabolic by-product or a common mediator of ageing signals? Nat Rev Mol Cell Biol 8:722-728.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 722-728
    • Giorgio, M.1    Trinei, M.2    Migliaccio, E.3    Pelicci, P.G.4
  • 28
    • 20144369335 scopus 로고    scopus 로고
    • Mitochondrial membrane depolarization and the selective death of dopaminergic neurons by rotenone: Protective effect of coenzyme Q10
    • Moon Y, Lee KH, Park JH, Geum D, Kim K (2005) Mitochondrial membrane depolarization and the selective death of dopaminergic neurons by rotenone: Protective effect of coenzyme Q10. J Neurochem 93:1199-1208.
    • (2005) J Neurochem , vol.93 , pp. 1199-1208
    • Moon, Y.1    Lee, K.H.2    Park, J.H.3    Geum, D.4    Kim, K.5
  • 29
    • 0344198025 scopus 로고    scopus 로고
    • Mechanism of toxicity in rotenone models of Parkinson's disease
    • Sherer TB, et al. (2003) Mechanism of toxicity in rotenone models of Parkinson's disease. J Neurosci 23:10756-10764.
    • (2003) J Neurosci , vol.23 , pp. 10756-10764
    • Sherer, T.B.1
  • 30
    • 0022628376 scopus 로고
    • Molecular architecture of the inner membrane of mitochondria from rat liver: A combined biochemical and stereological study
    • Schwerzmann K, Cruz-Orive LM, Eggman R, Sänger A, Weibel ER (1986) Molecular architecture of the inner membrane of mitochondria from rat liver: A combined biochemical and stereological study. J Cell Biol 102:97-103.
    • (1986) J Cell Biol , vol.102 , pp. 97-103
    • Schwerzmann, K.1    Cruz-Orive, L.M.2    Eggman, R.3    Sänger, A.4    Weibel, E.R.5
  • 31
  • 33
    • 0036172167 scopus 로고    scopus 로고
    • Geno3D: Automatic comparative molecular modelling of protein
    • Combet C, Jambon M, Deléage G, Geourjon C (2002) Geno3D: Automatic comparative molecular modelling of protein. Bioinformatics 18:213-214.
    • (2002) Bioinformatics , vol.18 , pp. 213-214
    • Combet, C.1    Jambon, M.2    Deléage, G.3    Geourjon, C.4
  • 34
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G (1990) WHAT IF: A molecular modeling and drug design program. J Mol Graphics 8:52-56.
    • (1990) J Mol Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 35
    • 0029781871 scopus 로고    scopus 로고
    • In vitro evaluation of a series of N-dodecanoyl-L-amino acid methyl esters as dermal penetration enhancers
    • Fincher TK, Yoo SD, Player MR, Sowell JW, Michniak BB (1996) In vitro evaluation of a series of N-dodecanoyl-L-amino acid methyl esters as dermal penetration enhancers. J Pharmacol Sci 85:920-923.
    • (1996) J Pharmacol Sci , vol.85 , pp. 920-923
    • Fincher, T.K.1    Yoo, S.D.2    Player, M.R.3    Sowell, J.W.4    Michniak, B.B.5
  • 36
    • 0033529941 scopus 로고    scopus 로고
    • The antioxidant neuroprotective effects of estrogens and phenolic compounds are independent from their estrogenic properties
    • Moosmann B, Behl C (1999) The antioxidant neuroprotective effects of estrogens and phenolic compounds are independent from their estrogenic properties. Proc Natl Acad Sci USA 96:8867-8872.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8867-8872
    • Moosmann, B.1    Behl, C.2
  • 37
    • 0041920608 scopus 로고    scopus 로고
    • Brain region-specific neuroprotective action and signaling of corticotropin-releasing hormone in primary neurons
    • Bayatti N, Zschocke J, Behl C (2003) Brain region-specific neuroprotective action and signaling of corticotropin-releasing hormone in primary neurons. Endocrinology 144:4051-4060.
    • (2003) Endocrinology , vol.144 , pp. 4051-4060
    • Bayatti, N.1    Zschocke, J.2    Behl, C.3
  • 38
    • 0035198214 scopus 로고    scopus 로고
    • Protective activity of aromatic amines and imines against oxidative nerve cell death
    • Moosmann B, Skutella T, Beyer K, Behl C (2001) Protective activity of aromatic amines and imines against oxidative nerve cell death. Biol Chem 382:1601-1612.
    • (2001) Biol Chem , vol.382 , pp. 1601-1612
    • Moosmann, B.1    Skutella, T.2    Beyer, K.3    Behl, C.4
  • 39
    • 0037687985 scopus 로고    scopus 로고
    • Selenoprotein N: An endoplasmic reticulum glycoprotein with a nearly developmental expression pattern
    • Petit N, et al. (2003) Selenoprotein N: An endoplasmic reticulum glycoprotein with a nearly developmental expression pattern. Hum Mol Genet 12:1045-1053.
    • (2003) Hum Mol Genet , vol.12 , pp. 1045-1053
    • Petit, N.1
  • 40
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37:911-917.
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 41
    • 0024291460 scopus 로고
    • Automated solid-phase catalyzed pre-column derivatization of fatty acids for reversed-phase high-performance liquid chromatographic analysis with fluorescence detection
    • Wolf JH, Korf J (1988) Automated solid-phase catalyzed pre-column derivatization of fatty acids for reversed-phase high-performance liquid chromatographic analysis with fluorescence detection. J Chromatogr 436:437-445.
    • (1988) J Chromatogr , vol.436 , pp. 437-445
    • Wolf, J.H.1    Korf, J.2
  • 42
    • 0026643731 scopus 로고
    • Inhibitory effect of eugenol on non-enzymatic lipid peroxidation in rat liver mitochondria
    • Nagababu E, Lakshmaiah N (1992) Inhibitory effect of eugenol on non-enzymatic lipid peroxidation in rat liver mitochondria. Biochem Pharmacol 43:2393-2400.
    • (1992) Biochem Pharmacol , vol.43 , pp. 2393-2400
    • Nagababu, E.1    Lakshmaiah, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.