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Volumn 2, Issue 4, 2003, Pages 809-820

POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELLS, CULTURED; COPPER; DNA, MITOCHONDRIAL; ENERGY METABOLISM; ESCHERICHIA COLI; MITOCHONDRIA; MITOCHONDRIAL DISEASES; MUTATION; NAD; OXIDATIVE STRESS; PHOSPHORYLATION; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); REACTIVE OXYGEN SPECIES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0043234233     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.2.4.809-820.2003     Document Type: Article
Times cited : (99)

References (84)
  • 2
    • 0033040503 scopus 로고    scopus 로고
    • Hydrogen peroxide causes significant mitochondrial DNA damage in human RPE cells
    • Ballinger, S. W., B. Van Houten, G. F. Jin, C. A. Conkiin, and B. F. Godley. 1999. Hydrogen peroxide causes significant mitochondrial DNA damage in human RPE cells. Exp. Eye Res. 68:765-772.
    • (1999) Exp. Eye Res. , vol.68 , pp. 765-772
    • Ballinger, S.W.1    Van Houten, B.2    Jin, G.F.3    Conkiin, C.A.4    Godley, B.F.5
  • 3
    • 0025785410 scopus 로고
    • A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors
    • Bonneaud, N., O. Ozier-Kalogeropoulos, G. Y. Li, M. Labouesse, L. Minvielle-Sebastia, and F. Lacroute. 1991. A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7:609-615.
    • (1991) Yeast , vol.7 , pp. 609-615
    • Bonneaud, N.1    Ozier-Kalogeropoulos, O.2    Li, G.Y.3    Labouesse, M.4    Minvielle-Sebastia, L.5    Lacroute, F.6
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0028341061 scopus 로고
    • Evidence for two NAD kinases in Salmonella typhimurium
    • Cheng, W., and J. R. Roth. 1994. Evidence for two NAD kinases in Salmonella typhimurium. J. Bacteriol. 176:4260-4268.
    • (1994) J. Bacteriol. , vol.176 , pp. 4260-4268
    • Cheng, W.1    Roth, J.R.2
  • 6
    • 0037303781 scopus 로고    scopus 로고
    • Searching for nuclear-mitochondrial genes
    • Chinnery, P. F. 2003. Searching for nuclear-mitochondrial genes. Trends Genet. 19:60-62.
    • (2003) Trends Genet. , vol.19 , pp. 60-62
    • Chinnery, P.F.1
  • 7
    • 0029087855 scopus 로고
    • MitoProt, a Macintosh application for studying mitochondrial proteins
    • Claros, M. G. 1995. MitoProt, a Macintosh application for studying mitochondrial proteins. Comput. Appl. Biosci. 11:441-447.
    • (1995) Comput. Appl. Biosci. , vol.11 , pp. 441-447
    • Claros, M.G.1
  • 8
    • 0032805796 scopus 로고    scopus 로고
    • Mitochondrial DNA repair pathways
    • Croteau, D. L., R. H. Stierum, and V. A. Bohr. 1999. Mitochondrial DNA repair pathways. Mutat. Res. 434:137-148.
    • (1999) Mutat. Res. , vol.434 , pp. 137-148
    • Croteau, D.L.1    Stierum, R.H.2    Bohr, V.A.3
  • 10
    • 0037064058 scopus 로고    scopus 로고
    • Biochemistry of mitochondrial nitric-oxide synthase
    • Elfering, S. L., T. M. Sarkela, and C. Giulivi. 2002. Biochemistry of mitochondrial nitric-oxide synthase. J. Biol. Chem. 277:38079-38086.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38079-38086
    • Elfering, S.L.1    Sarkela, T.M.2    Giulivi, C.3
  • 11
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., H. Nielsen, S. Brunak, and G. von Heijne. 2000. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300:1005-1016.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 12
    • 0031128356 scopus 로고    scopus 로고
    • The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver
    • Esworthy, R. S., Y. S. Ho, and F. F. Chu. 1997. The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver. Arch. Biochem. Biophys. 340:59-63.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 59-63
    • Esworthy, R.S.1    Ho, Y.S.2    Chu, F.F.3
  • 14
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. 1995. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64:97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 15
    • 0037184525 scopus 로고    scopus 로고
    • How to flip the (redox) switch
    • Georgiou, G. 2002. How to flip the (redox) switch. Cell 111:607-610.
    • (2002) Cell , vol.111 , pp. 607-610
    • Georgiou, G.1
  • 16
    • 0033609012 scopus 로고    scopus 로고
    • Pathways of As(III) detoxification in Saccharomyces cerevisiae
    • Ghosh, M., J. Shen, and B. P. Rosen. 1999. Pathways of As(III) detoxification in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 96:5001-5006.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5001-5006
    • Ghosh, M.1    Shen, J.2    Rosen, B.P.3
  • 17
    • 0037441389 scopus 로고    scopus 로고
    • Characterization and function of mitochondrial nitric-oxide synthase
    • Giulivi, C. 2003. Characterization and function of mitochondrial nitric-oxide synthase. Free Radic. Biol. Med. 34:397-408.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 397-408
    • Giulivi, C.1
  • 18
    • 0026046097 scopus 로고
    • ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene
    • Gralla, E. B., D. J. Thiele, P. Silar, and J. S. Valentine. 1991. ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene. Proc. Natl. Acad. Sci. USA 88:8558-8562.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8558-8562
    • Gralla, E.B.1    Thiele, D.J.2    Silar, P.3    Valentine, J.S.4
  • 19
    • 0036639779 scopus 로고    scopus 로고
    • The mitochondrial DNA polymerase as a target of oxidative damage
    • Graziewicz, M. A., B. J. Day, and W. C. Copeland. 2002. The mitochondrial DNA polymerase as a target of oxidative damage. Nucleic Acids Res. 30:2817-2824.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2817-2824
    • Graziewicz, M.A.1    Day, B.J.2    Copeland, W.C.3
  • 20
    • 0242677926 scopus 로고    scopus 로고
    • SOS-dependent A→G transitions induced by hydroxyl radical generating system hypoxanthine/xanthine oxidase/Fe3+/EDTA are accompanied by the increase of Fapy-adenine content in M13 mp18 phage DNA
    • Graziewicz, M. A., T. H. Zastawny, R. Olinski, and B. Tudek. 1999. SOS-dependent A→G transitions induced by hydroxyl radical generating system hypoxanthine/xanthine oxidase/Fe3+/EDTA are accompanied by the increase of Fapy-adenine content in M13 mp18 phage DNA. Mutat. Res. 434:41-52.
    • (1999) Mutat. Res. , vol.434 , pp. 41-52
    • Graziewicz, M.A.1    Zastawny, T.H.2    Olinski, R.3    Tudek, B.4
  • 22
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • Holmgren, A., and M. Bjornstedt. 1995. Thioredoxin and thioredoxin reductase. Methods Enzymol. 252:199-208.
    • (1995) Methods Enzymol. , vol.252 , pp. 199-208
    • Holmgren, A.1    Bjornstedt, M.2
  • 23
    • 0028223175 scopus 로고
    • Physiological characterization of the yeast metallothionein (CUP1) promoter, and consequences of overexpressing its transcriptional activator, ACE1
    • Hottiger, T., P. Furst, G. Pohlig, and J. Heim. 1994. Physiological characterization of the yeast metallothionein (CUP1) promoter, and consequences of overexpressing its transcriptional activator, ACE1. Yeast 10:283-296.
    • (1994) Yeast , vol.10 , pp. 283-296
    • Hottiger, T.1    Furst, P.2    Pohlig, G.3    Heim, J.4
  • 24
    • 0024500781 scopus 로고
    • Characterization of NADH kinase from Saccharomyces cerevisiae
    • Tokyo
    • Iwahashi, Y., A. Hitoshio, N. Tajima, and T. Nakamura. 1989. Characterization of NADH kinase from Saccharomyces cerevisiae. J. Biochem. (Tokyo) 105:588-593.
    • (1989) J. Biochem. , vol.105 , pp. 588-593
    • Iwahashi, Y.1    Hitoshio, A.2    Tajima, N.3    Nakamura, T.4
  • 25
    • 0027066743 scopus 로고
    • In vivo evidence of hydroxyl radical formation after acute copper and ascorbic acid intake: Electron spin resonance spin-trapping investigation
    • Kadiiska, M. B., P. M. Hanna, L. Hernandez, and R. P. Mason. 1992. In vivo evidence of hydroxyl radical formation after acute copper and ascorbic acid intake: electron spin resonance spin-trapping investigation. Mol. Pharmacol. 42:723-729.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 723-729
    • Kadiiska, M.B.1    Hanna, P.M.2    Hernandez, L.3    Mason, R.P.4
  • 27
    • 0034833016 scopus 로고    scopus 로고
    • Molecular characterization of Escherichia coli NAD kinase
    • Kawai, S., S. Mori, T. Mukai, W. Hashimoto, and K. Murata. 2001. Molecular characterization of Escherichia coli NAD kinase. Eur. J. Biochem. 268:4359-4365.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4359-4365
    • Kawai, S.1    Mori, S.2    Mukai, T.3    Hashimoto, W.4    Murata, K.5
  • 29
    • 0035948228 scopus 로고    scopus 로고
    • Molecular cloning and identification of UTR1 of a yeast Saccharomyces cerevisiae as a gene encoding an NAD kinase
    • Kawai, S., S. Suzuki, S. Mori, and K. Murata. 2001. Molecular cloning and identification of UTR1 of a yeast Saccharomyces cerevisiae as a gene encoding an NAD kinase. FEMS Microbiol. Lett. 200:181-184.
    • (2001) FEMS Microbiol. Lett. , vol.200 , pp. 181-184
    • Kawai, S.1    Suzuki, S.2    Mori, S.3    Murata, K.4
  • 30
    • 0009424743 scopus 로고
    • Catalase: A tetrameric enzyme with four tightly bound molecules of NADPH
    • Kirkman, H. N., and G. F. Gaetani. 1984. Catalase: a tetrameric enzyme with four tightly bound molecules of NADPH. Proc. Natl. Acad. Sci. USA 81:4343-4347.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4343-4347
    • Kirkman, H.N.1    Gaetani, G.F.2
  • 31
    • 0033553562 scopus 로고    scopus 로고
    • Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry
    • Kirkman, H. N., M. Rolfo, A. M. Ferraris, and G. F. Gaetani. 1999. Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry. J. Biol. Chem. 274:13908-13914.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13908-13914
    • Kirkman, H.N.1    Rolfo, M.2    Ferraris, A.M.3    Gaetani, G.F.4
  • 32
    • 0028906080 scopus 로고
    • Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress
    • Krems, B., C. Charizanis, and K. D. Entian. 1995. Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress. Curr. Genet. 27:427-434.
    • (1995) Curr. Genet. , vol.27 , pp. 427-434
    • Krems, B.1    Charizanis, C.2    Entian, K.D.3
  • 34
    • 0001313535 scopus 로고
    • The distribution of the number of mutants in bacterial populations
    • Lea, D. E., and C. A. Coulson. 1949. The distribution of the number of mutants in bacterial populations. J. Genet. 49:264-285.
    • (1949) J. Genet. , vol.49 , pp. 264-285
    • Lea, D.E.1    Coulson, C.A.2
  • 35
    • 0032806595 scopus 로고    scopus 로고
    • Repair of alkylation and oxidative damage in mitochondrial DNA
    • LeDoux, S. P., W. J. Driggers, B. S. Hollensworth, and G. L. Wilson. 1999. Repair of alkylation and oxidative damage in mitochondrial DNA. Mutat. Res. 434:149-159.
    • (1999) Mutat. Res. , vol.434 , pp. 149-159
    • LeDoux, S.P.1    Driggers, W.J.2    Hollensworth, B.S.3    Wilson, G.L.4
  • 36
    • 0026493929 scopus 로고
    • Repair of mitochondrial DNA after various types of DNA damage in Chinese hamster ovary cells
    • LeDoux, S. P., G. L. Wilson, E. J. Beecham, T. Stevnsner, K. Wassermann, and V. A. Bohr. 1992. Repair of mitochondrial DNA after various types of DNA damage in Chinese hamster ovary cells. Carcinogenesis 13:1967-1973.
    • (1992) Carcinogenesis , vol.13 , pp. 1967-1973
    • LeDoux, S.P.1    Wilson, G.L.2    Beecham, E.J.3    Stevnsner, T.4    Wassermann, K.5    Bohr, V.A.6
  • 37
  • 40
    • 0032555281 scopus 로고    scopus 로고
    • Characterization of the native and recombinant catalytic subunit of human DNA polymerase gamma: Identification of residues critical for exonuclease activity and dideoxynucleotide sensitivity
    • Longley, M. J., P. A. Ropp, S. E. Lim, and W. C. Copeland. 1998. Characterization of the native and recombinant catalytic subunit of human DNA polymerase gamma: identification of residues critical for exonuclease activity and dideoxynucleotide sensitivity. Biochemistry 37:10529-10539.
    • (1998) Biochemistry , vol.37 , pp. 10529-10539
    • Longley, M.J.1    Ropp, P.A.2    Lim, S.E.3    Copeland, W.C.4
  • 41
    • 0001641514 scopus 로고
    • Mutations of bacteria from virus sensitivity to virus resistance
    • Luria, S. E., and M. Delbruck. 1943. Mutations of bacteria from virus sensitivity to virus resistance. Genetics 28:491-511.
    • (1943) Genetics , vol.28 , pp. 491-511
    • Luria, S.E.1    Delbruck, M.2
  • 43
    • 0027494167 scopus 로고
    • The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of Saccharomyces cerevisiae share a common ancestry
    • Melnick, L., and F. Sherman. 1993. The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of Saccharomyces cerevisiae share a common ancestry. J. Mol. Biol. 233:372-388.
    • (1993) J. Mol. Biol. , vol.233 , pp. 372-388
    • Melnick, L.1    Sherman, F.2
  • 44
    • 0036469120 scopus 로고    scopus 로고
    • Regulation of mitochondrial thioredoxin peroxidase I expression by two different pathways: One dependent on cAMP and the other on heme
    • Monteiro, G., G. A. Pereira, and L. E. Netto. 2002. Regulation of mitochondrial thioredoxin peroxidase I expression by two different pathways: one dependent on cAMP and the other on heme. Free Radic. Biol. Med. 32:278-288.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 278-288
    • Monteiro, G.1    Pereira, G.A.2    Netto, L.E.3
  • 46
    • 0037068964 scopus 로고    scopus 로고
    • Clinical importance of the cytochromes P450
    • Nebert, D. W., and D. W. Russell. 2002. Clinical importance of the cytochromes P450. Lancet 360:1155-1162.
    • (2002) Lancet , vol.360 , pp. 1155-1162
    • Nebert, D.W.1    Russell, D.W.2
  • 47
    • 0037026866 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase 1 protects Saccharomyces cerevisiae against metal ion toxicity and glutathione depletion
    • Nguyen-nhu, N. T., and B. Knoops. 2002. Alkyl hydroperoxide reductase 1 protects Saccharomyces cerevisiae against metal ion toxicity and glutathione depletion. Toxicol. Lett. 135:219-228.
    • (2002) Toxicol. Lett. , vol.135 , pp. 219-228
    • Nguyen-nhu, N.T.1    Knoops, B.2
  • 48
    • 0030963238 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in hepatocytes induced by t-BuOOH: NAD(P)H and reactive oxygen species
    • Nieminen, A. L., A. M. Byrne, B. Herman, and J. J. Lemasters. 1997. Mitochondrial permeability transition in hepatocytes induced by t-BuOOH: NAD(P) H and reactive oxygen species. Am. J. Physiol. 272:C1286-C1294.
    • (1997) Am. J. Physiol. , vol.272
    • Nieminen, A.L.1    Byrne, A.M.2    Herman, B.3    Lemasters, J.J.4
  • 49
    • 0033613865 scopus 로고    scopus 로고
    • Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder
    • Nishino, I., A. Spinazzola, and M. Hirano. 1999. Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder. Science 283:689-692.
    • (1999) Science , vol.283 , pp. 689-692
    • Nishino, I.1    Spinazzola, A.2    Hirano, M.3
  • 51
    • 0036258184 scopus 로고    scopus 로고
    • Mitochondrial dysfunction due to oxidative mitochondrial DNA damage is reduced through cooperative actions of diverse proteins
    • O'Rourke, T. W., N. A. Doudican, M. D. Mackereth, P. W. Doetsch, and G. S. Shadel. 2002. Mitochondrial dysfunction due to oxidative mitochondrial DNA damage is reduced through cooperative actions of diverse proteins. Mol. Cell. Biol. 22:4086-4093.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4086-4093
    • O'Rourke, T.W.1    Doudican, N.A.2    Mackereth, M.D.3    Doetsch, P.W.4    Shadel, G.S.5
  • 52
    • 0037881908 scopus 로고    scopus 로고
    • A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae
    • Outten, C. E., and V. C. Culotta. 2003. A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae. EMBO J. 22:2015-2024.
    • (2003) EMBO J. , vol.22 , pp. 2015-2024
    • Outten, C.E.1    Culotta, V.C.2
  • 53
    • 0000056465 scopus 로고    scopus 로고
    • Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae
    • Park, S. G., M. K. Cha, W. Jeong, and I. H. Kim. 2000. Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae. J. Biol. Chem. 275:5723-5732.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5723-5732
    • Park, S.G.1    Cha, M.K.2    Jeong, W.3    Kim, I.H.4
  • 54
    • 0034717135 scopus 로고    scopus 로고
    • Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity
    • Pedrajas, J. R., A. Miranda-Vizuete, N. Javanmardy, J. A. Gustafsson, and G. Spyrou. 2000. Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity. J. Biol. Chem. 275:16296-16301.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16296-16301
    • Pedrajas, J.R.1    Miranda-Vizuete, A.2    Javanmardy, N.3    Gustafsson, J.A.4    Spyrou, G.5
  • 55
    • 0037474277 scopus 로고    scopus 로고
    • NAD(P)H, a primary target of 1O2 in mitochondria of intact cells
    • Petrat, F., S. Pindiur, M. Kirsch, and H. De Groot. 2003. NAD(P)H, a primary target of 1O2 in mitochondria of intact cells. J. Biol. Chem. 278:3298-3307.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3298-3307
    • Petrat, F.1    Pindiur, S.2    Kirsch, M.3    De Groot, H.4
  • 56
    • 0031952184 scopus 로고    scopus 로고
    • Efficient repair of abasic sites in DNA by mitochondrial enzymes
    • Pinz, K. G., and D. F. Bogenhagen. 1998. Efficient repair of abasic sites in DNA by mitochondrial enzymes. Mol. Cell. Biol. 18:1257-1265.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1257-1265
    • Pinz, K.G.1    Bogenhagen, D.F.2
  • 57
    • 0037013234 scopus 로고    scopus 로고
    • Active site mutation in DNA polymerase gamma associated with progressive external ophthalmoplegia causes error-prone DNA synthesis
    • Ponamarev, M. V., M. J. Longley, D. Nguyen, T. A. Kunkel, and W. C. Copeland. 2002 Active site mutation in DNA polymerase gamma associated with progressive external ophthalmoplegia causes error-prone DNA synthesis. J. Biol. Chem. 277:15225-15228.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15225-15228
    • Ponamarev, M.V.1    Longley, M.J.2    Nguyen, D.3    Kunkel, T.A.4    Copeland, W.C.5
  • 58
    • 0023811053 scopus 로고
    • Normal oxidative damage to mitochondrial and nuclear DNA is extensive
    • Richter, C., J. W. Park, and B. N. Ames. 1988. Normal oxidative damage to mitochondrial and nuclear DNA is extensive. Proc. Natl. Acad. Sci. USA 85:6465-6467.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6465-6467
    • Richter, C.1    Park, J.W.2    Ames, B.N.3
  • 59
    • 0030587492 scopus 로고    scopus 로고
    • Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma
    • Ropp, P. A., and W. C. Copeland. 1996. Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma. Genomics 36:449-458.
    • (1996) Genomics , vol.36 , pp. 449-458
    • Ropp, P.A.1    Copeland, W.C.2
  • 60
    • 0035179561 scopus 로고    scopus 로고
    • Mutant mitochondrial thymidine kinase in mitochondrial DNA depletion myopathy
    • Saada, A., A. Shaag, H. Mandel, Y. Nevo, S. Eriksson, and O. Elpeleg. 2001. Mutant mitochondrial thymidine kinase in mitochondrial DNA depletion myopathy. Nat. Genet. 29:342-344.
    • (2001) Nat. Genet. , vol.29 , pp. 342-344
    • Saada, A.1    Shaag, A.2    Mandel, H.3    Nevo, Y.4    Eriksson, S.5    Elpeleg, O.6
  • 61
    • 0031441858 scopus 로고    scopus 로고
    • Preferential mitochondrial DNA injury caused by glucose oxidase as a steady generator of hydrogen peroxide in human fibroblasts
    • Salazar, J. J., and B. Van Houten. 1997. Preferential mitochondrial DNA injury caused by glucose oxidase as a steady generator of hydrogen peroxide in human fibroblasts. Mutat. Res. 385:139-149.
    • (1997) Mutat. Res. , vol.385 , pp. 139-149
    • Salazar, J.J.1    Van Houten, B.2
  • 62
    • 0037449724 scopus 로고    scopus 로고
    • Cell sorting experiments link persistent mitochondrial DNA damage with loss of mitochondrial membrane potential and apoptotic cell death
    • Santos, J. H., L. Hunakova, Y. Chen, C. Bortner, and B. Van Houten. 2003. Cell sorting experiments link persistent mitochondrial DNA damage with loss of mitochondrial membrane potential and apoptotic cell death. J. Biol. Chem. 278:1728-1734.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1728-1734
    • Santos, J.H.1    Hunakova, L.2    Chen, Y.3    Bortner, C.4    Van Houten, B.5
  • 63
    • 0036322455 scopus 로고    scopus 로고
    • Cofactors of mitochondrial enzymes attenuate copper-induced death in vitro and in vivo
    • Sheline, C. T., E. H. Choi, J. S. Kim-Han, L. L. Dugan, and D. W. Choi. 2002. Cofactors of mitochondrial enzymes attenuate copper-induced death in vitro and in vivo. Ann. Neurol. 52:195-204.
    • (2002) Ann. Neurol. , vol.52 , pp. 195-204
    • Sheline, C.T.1    Choi, E.H.2    Kim-Han, J.S.3    Dugan, L.L.4    Choi, D.W.5
  • 64
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. 1991. Getting started with yeast. Methods Enzymol. 194:3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 66
    • 0028116159 scopus 로고
    • Effect of age and caloric restriction on DNA oxidative damage in different tissues of C57BL/6 mice
    • Sohal, R. S., S. Agarwal, M. Candas, M. J. Forster, and H. Lal. 1994. Effect of age and caloric restriction on DNA oxidative damage in different tissues of C57BL/6 mice. Mech. Ageing Dev. 76:215-224.
    • (1994) Mech. Ageing Dev. , vol.76 , pp. 215-224
    • Sohal, R.S.1    Agarwal, S.2    Candas, M.3    Forster, M.J.4    Lal, H.5
  • 68
    • 0028065054 scopus 로고
    • Yeast kar1 mutants provide an effective method for YAC transfer to new hosts
    • Spencer, F., Y. Hugerat, G. Simchen, O. Hurko, C. Connelly, and P. Hieter. 1994. Yeast kar1 mutants provide an effective method for YAC transfer to new hosts. Genomics 22:118-126.
    • (1994) Genomics , vol.22 , pp. 118-126
    • Spencer, F.1    Hugerat, Y.2    Simchen, G.3    Hurko, O.4    Connelly, C.5    Hieter, P.6
  • 69
    • 0029904234 scopus 로고    scopus 로고
    • Expression of a recoded nuclear gene inserted into yeast mitochondrial DNA is limited by mRNA-specific translational activation
    • Steele, D. F., C. A. Butler, and T. D. Fox. 1996. Expression of a recoded nuclear gene inserted into yeast mitochondrial DNA is limited by mRNA-specific translational activation. Proc. Natl. Acad. Sci. USA 93:5253-5257.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5253-5257
    • Steele, D.F.1    Butler, C.A.2    Fox, T.D.3
  • 71
    • 0029977674 scopus 로고    scopus 로고
    • Copper ions and the regulation of Saccharomyces cerevisiae metallothionein genes under aerobic and anaerobic conditions
    • Strain, J., and V. C. Culotta. 1996. Copper ions and the regulation of Saccharomyces cerevisiae metallothionein genes under aerobic and anaerobic conditions. Mol. Gen. Genet. 251:139-145.
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 139-145
    • Strain, J.1    Culotta, V.C.2
  • 72
    • 0036361563 scopus 로고    scopus 로고
    • Measuring mtDNA mutation rates in Saccharomyces cerevisiae using the mtArg8 assay
    • Strand, M. K., and W. C. Copeland. 2002. Measuring mtDNA mutation rates in Saccharomyces cerevisiae using the mtArg8 assay. Methods Mol. Biol. 197:151-157.
    • (2002) Methods Mol. Biol. , vol.197 , pp. 151-157
    • Strand, M.K.1    Copeland, W.C.2
  • 73
    • 0031577469 scopus 로고    scopus 로고
    • Gene structure for mouse glutathione reductase, including a putative mitochondrial targeting signal
    • Tamura, T., H. W. McMicken, C. V. Smith, and T. N. Hansen. 1997. Gene structure for mouse glutathione reductase, including a putative mitochondrial targeting signal. Biochem. Biophys. Res. Commun. 237:419-422.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 419-422
    • Tamura, T.1    McMicken, H.W.2    Smith, C.V.3    Hansen, T.N.4
  • 74
    • 0024044018 scopus 로고
    • ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene
    • Thiele, D. J. 1988. ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene. Mol. Cell. Biol. 8:2745-2752.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2745-2752
    • Thiele, D.J.1
  • 75
    • 0030962035 scopus 로고    scopus 로고
    • Hypermutability of homonucleotide runs in mismatch repair and DNA polymerase proofreading yeast mutants
    • Tran, H. T., J. D. Keen, M. Kricker, M. A. Resnick, and D. A. Gordenin. 1997. Hypermutability of homonucleotide runs in mismatch repair and DNA polymerase proofreading yeast mutants. Mol. Cell. Biol. 17:2859-2865.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2859-2865
    • Tran, H.T.1    Keen, J.D.2    Kricker, M.3    Resnick, M.A.4    Gordenin, D.A.5
  • 76
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens, J. F., and A. Boveris. 1980. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191:421-427.
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 77
    • 0034943967 scopus 로고    scopus 로고
    • Mutation of POLG is associated with progressive external ophthalmoplegia characterized by mtDNA deletions
    • Van Goethem, G., B. Dermaut, A. Lofgren, J. J. Martin, and C. Van Broeckhoven. 2001. Mutation of POLG is associated with progressive external ophthalmoplegia characterized by mtDNA deletions. Nat. Genet. 28:211-212.
    • (2001) Nat. Genet. , vol.28 , pp. 211-212
    • Van Goethem, G.1    Dermaut, B.2    Lofgren, A.3    Martin, J.J.4    Van Broeckhoven, C.5
  • 78
    • 0033916954 scopus 로고    scopus 로고
    • Further evidence for genetic heterogeneity of autosomal dominant disorders with accumulation of multiple deletions of mitochondrial DNA
    • Van Goethem, G., A. Lofgren, J. J. Martin, and C. Van Broeckhoven. 2000. Further evidence for genetic heterogeneity of autosomal dominant disorders with accumulation of multiple deletions of mitochondrial DNA. J. Med. Genet. 37:547-548.
    • (2000) J. Med. Genet. , vol.37 , pp. 547-548
    • Van Goethem, G.1    Lofgren, A.2    Martin, J.J.3    Van Broeckhoven, C.4
  • 79
    • 0026624980 scopus 로고
    • Diseases of the mitochondrial DNA
    • Wallace, D. C. 1992. Diseases of the mitochondrial DNA. Annu. Rev. Biochem. 61:1175-1212.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1175-1212
    • Wallace, D.C.1
  • 80
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace, D. C. 1999. Mitochondrial diseases in man and mouse. Science 283:1482-1488.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 82
    • 0019891031 scopus 로고
    • Ubisemiquinone radicals from the cytochrome b-c1 complex of the mitochondrial electron transport chain - Demonstration of QP-S radical formation
    • Wei, Y., C. P. Scholes, and T. E. King. 1981. Ubisemiquinone radicals from the cytochrome b-c1 complex of the mitochondrial electron transport chain - demonstration of QP-S radical formation. Biochem. Biophys. Res. Commun. 99:1411-1419.
    • (1981) Biochem. Biophys. Res. Commun. , vol.99 , pp. 1411-1419
    • Wei, Y.1    Scholes, C.P.2    King, T.E.3
  • 83
    • 0031032817 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress
    • Yakes, F. M., and B. Van Houten. 1997. Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress. Proc. Natl. Acad. Sci. USA 94:514-519.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 514-519
    • Yakes, F.M.1    Van Houten, B.2
  • 84
    • 0028132589 scopus 로고
    • Ribonucleotide reductase: Evidence for specific association with HeLa cell mitochondria
    • Young, P., J. M. Leeds, M. B. Slabaugh, and C. K. Mathews. 1994. Ribonucleotide reductase: evidence for specific association with HeLa cell mitochondria. Biochem. Biophys. Res. Commun. 203:46-52.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 46-52
    • Young, P.1    Leeds, J.M.2    Slabaugh, M.B.3    Mathews, C.K.4


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