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Volumn 1841, Issue 4, 2014, Pages 630-644

Coenzyme Q supplementation or over-expression of the yeast Coq8 putative kinase stabilizes multi-subunit Coq polypeptide complexes in yeast coq null mutants

Author keywords

Coenzyme Q supplementation; Mitochondrial metabolism; Protein complex; Q biosynthetic intermediate; Saccharomyces cerevisiae; Ubiquinone

Indexed keywords

CHAPERONIN 60; COQ10 POLYPEPTIDE; COQ3 POLYPEPTIDE; COQ4 POLYPEPTIDE; COQ5 POLYPEPTIDE; COQ6 POLYPEPTIDE; COQ7 POLYPEPTIDE; COQ9 POLYPEPTIDE; CYTOCHROME C; DIGITONIN; LACTATE DEHYDROGENASE (CYTOCHROME); MEMBRANE PROTEIN; POLYPEPTIDE; UBIQUINONE; UNCLASSIFIED DRUG; 3,4-DIHYDROXY-5-HEXAPRENYLBENZOATE METHYLTRANSFERASE; COQ10 PROTEIN, S CEREVISIAE; COQ4 PROTEIN, S CEREVISIAE; COQ5 PROTEIN, S CEREVISIAE; COQ8 PROTEIN, S CEREVISIAE; METHYLTRANSFERASE; MITOCHONDRIAL PROTEIN; MULTIPROTEIN COMPLEX; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUINONE 6; UBIQUINONE 7;

EID: 84895725183     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2013.12.017     Document Type: Article
Times cited : (85)

References (99)
  • 4
    • 0002127403 scopus 로고
    • A survey of the function and specificity of ubiquinone in the mitochondrial respiratory chain
    • G. Lenaz, John Wiley & Sons New York
    • G. Lenaz, and A. De Santis A survey of the function and specificity of ubiquinone in the mitochondrial respiratory chain G. Lenaz, Coenzyme Q Biochemistry, Bioenergetics and Clinical Applications of Ubiquinone 1985 John Wiley & Sons New York 165 199
    • (1985) Coenzyme Q Biochemistry, Bioenergetics and Clinical Applications of Ubiquinone , pp. 165-199
    • Lenaz, G.1    De Santis, A.2
  • 5
    • 44949214775 scopus 로고    scopus 로고
    • Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria
    • T.M. Hildebrandt, and M.K. Grieshaber Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria FEBS J. 275 2008 3352 3361
    • (2008) FEBS J. , vol.275 , pp. 3352-3361
    • Hildebrandt, T.M.1    Grieshaber, M.K.2
  • 10
    • 84873399755 scopus 로고    scopus 로고
    • Effect of coenzyme Q10 supplementation on heart failure: A meta-analysis
    • A.D. Fotino, A.M. Thompson-Paul, and L.A. Bazzano Effect of coenzyme Q10 supplementation on heart failure: a meta-analysis Am. J. Clin. Nutr. 97 2013 268 275
    • (2013) Am. J. Clin. Nutr. , vol.97 , pp. 268-275
    • Fotino, A.D.1    Thompson-Paul, A.M.2    Bazzano, L.A.3
  • 12
    • 34248195476 scopus 로고    scopus 로고
    • Endogenous synthesis of coenzyme Q in eukaryotes
    • (Supplement)
    • U.C. Tran, and C.F. Clarke Endogenous synthesis of coenzyme Q in eukaryotes Mitochondrion 7 2007 S62 S71 (Supplement)
    • (2007) Mitochondrion , vol.7
    • Tran, U.C.1    Clarke, C.F.2
  • 14
    • 84872966586 scopus 로고    scopus 로고
    • Molecular genetics of ubiquinone biosynthesis in animals
    • Y. Wang, and S. Hekimi Molecular genetics of ubiquinone biosynthesis in animals Crit. Rev. Biochem. Mol. Biol. 48 2013 69 88
    • (2013) Crit. Rev. Biochem. Mol. Biol. , vol.48 , pp. 69-88
    • Wang, Y.1    Hekimi, S.2
  • 16
    • 80053160231 scopus 로고    scopus 로고
    • Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation reaction and substrate analogs rescue Coq6 deficiency
    • M. Ozeir, U. Muhlenhoff, H. Webert, R. Lill, M. Fontecave, and F. Pierrel Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation reaction and substrate analogs rescue Coq6 deficiency Chem. Biol. 18 2011 1134 1142
    • (2011) Chem. Biol. , vol.18 , pp. 1134-1142
    • Ozeir, M.1    Muhlenhoff, U.2    Webert, H.3    Lill, R.4    Fontecave, M.5    Pierrel, F.6
  • 19
    • 57649178662 scopus 로고    scopus 로고
    • The yeast Coq4 polypeptide organizes a mitochondrial protein complex essential for coenzyme Q biosynthesis
    • B. Marbois, P. Gin, M. Gulmezian, and C.F. Clarke The yeast Coq4 polypeptide organizes a mitochondrial protein complex essential for coenzyme Q biosynthesis Biochim. Biophys. Acta 1791 2009 69 75
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 69-75
    • Marbois, B.1    Gin, P.2    Gulmezian, M.3    Clarke, C.F.4
  • 21
    • 55349084786 scopus 로고    scopus 로고
    • Ubiquinone biosynthesis in Saccharomyces cerevisiae: The molecular organization of O-methylase Coq3p depends on Abc1p/Coq8p
    • A. Tauche, U. Krause-Buchholz, and G. Rodel Ubiquinone biosynthesis in Saccharomyces cerevisiae: the molecular organization of O-methylase Coq3p depends on Abc1p/Coq8p FEMS Yeast Res. 8 2008 1263 1275
    • (2008) FEMS Yeast Res. , vol.8 , pp. 1263-1275
    • Tauche, A.1    Krause-Buchholz, U.2    Rodel, G.3
  • 22
    • 0030063759 scopus 로고    scopus 로고
    • The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis
    • B.N. Marbois, and C.F. Clarke The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis J. Biol. Chem. 271 1996 2995 3004
    • (1996) J. Biol. Chem. , vol.271 , pp. 2995-3004
    • Marbois, B.N.1    Clarke, C.F.2
  • 23
    • 33745205101 scopus 로고    scopus 로고
    • Complementation of Saccharomyces cerevisiae coq7 mutants by mitochondrial targeting of the Escherichia coli UbiF polypeptide: Two functions of yeast Coq7 polypeptide in coenzyme Q biosynthesis
    • U.C. Tran, B. Marbois, P. Gin, M. Gulmezian, T. Jonassen, and C.F. Clarke Complementation of Saccharomyces cerevisiae coq7 mutants by mitochondrial targeting of the Escherichia coli UbiF polypeptide: two functions of yeast Coq7 polypeptide in coenzyme Q biosynthesis J. Biol. Chem. 281 2006 16401 16409
    • (2006) J. Biol. Chem. , vol.281 , pp. 16401-16409
    • Tran, U.C.1    Marbois, B.2    Gin, P.3    Gulmezian, M.4    Jonassen, T.5    Clarke, C.F.6
  • 24
    • 0031722706 scopus 로고    scopus 로고
    • Novel families of putative protein kinases in bacteria and archaea: Evolution of the "eukaryotic" protein kinase superfamily
    • C.J. Leonard, L. Aravind, and E.V. Koonin Novel families of putative protein kinases in bacteria and archaea: evolution of the "eukaryotic" protein kinase superfamily Genome Res. 8 1998 1038 1047
    • (1998) Genome Res. , vol.8 , pp. 1038-1047
    • Leonard, C.J.1    Aravind, L.2    Koonin, E.V.3
  • 25
    • 0033820931 scopus 로고    scopus 로고
    • Identification of Escherichia coli ubiB, a gene required for the first monooxygenase step in ubiquinone biosynthesis
    • W.W. Poon, D.E. Davis, H.T. Ha, T. Jonassen, P.N. Rather, and C.F. Clarke Identification of Escherichia coli ubiB, a gene required for the first monooxygenase step in ubiquinone biosynthesis J. Bacteriol. 182 2000 5139 5146
    • (2000) J. Bacteriol. , vol.182 , pp. 5139-5146
    • Poon, W.W.1    Davis, D.E.2    Ha, H.T.3    Jonassen, T.4    Rather, P.N.5    Clarke, C.F.6
  • 26
    • 0035947594 scopus 로고    scopus 로고
    • A defect in coenzyme Q biosynthesis is responsible for the respiratory deficiency in Saccharomyces cerevisiae abc1 mutants
    • T.Q. Do, A.Y. Hsu, T. Jonassen, P.T. Lee, and C.F. Clarke A defect in coenzyme Q biosynthesis is responsible for the respiratory deficiency in Saccharomyces cerevisiae abc1 mutants J. Biol. Chem. 276 2001 18161 18168
    • (2001) J. Biol. Chem. , vol.276 , pp. 18161-18168
    • Do, T.Q.1    Hsu, A.Y.2    Jonassen, T.3    Lee, P.T.4    Clarke, C.F.5
  • 27
    • 0348049905 scopus 로고    scopus 로고
    • Pleiotropic phenotypes of fission yeast defective in ubiquinone-10 production. A study from the abc1Sp (coq8Sp) mutant
    • R. Saiki, Y. Ogiyama, T. Kainou, T. Nishi, H. Matsuda, and M. Kawamukai Pleiotropic phenotypes of fission yeast defective in ubiquinone-10 production. A study from the abc1Sp (coq8Sp) mutant Biofactors 18 2003 229 235
    • (2003) Biofactors , vol.18 , pp. 229-235
    • Saiki, R.1    Ogiyama, Y.2    Kainou, T.3    Nishi, T.4    Matsuda, H.5    Kawamukai, M.6
  • 30
    • 0032500832 scopus 로고    scopus 로고
    • Isolation of an Arabidopsis thaliana cDNA by complementation of a yeast abc1 deletion mutant deficient in complex III respiratory activity
    • B. Cardazzo, P. Hamel, W. Sakamoto, H. Wintz, and G. Dujardin Isolation of an Arabidopsis thaliana cDNA by complementation of a yeast abc1 deletion mutant deficient in complex III respiratory activity Gene 221 1998 117 125
    • (1998) Gene , vol.221 , pp. 117-125
    • Cardazzo, B.1    Hamel, P.2    Sakamoto, W.3    Wintz, H.4    Dujardin, G.5
  • 31
    • 79953795039 scopus 로고    scopus 로고
    • Expression of the human atypical kinase ADCK3 rescues coenzyme Q biosynthesis and phosphorylation of Coq polypeptides in yeast coq8 mutants
    • L.X. Xie, E.J. Hsieh, S. Watanabe, C.M. Allan, J.Y. Chen, U.C. Tran, and C.F. Clarke Expression of the human atypical kinase ADCK3 rescues coenzyme Q biosynthesis and phosphorylation of Coq polypeptides in yeast coq8 mutants Biochim. Biophys. Acta 1811 2011 348 360
    • (2011) Biochim. Biophys. Acta , vol.1811 , pp. 348-360
    • Xie, L.X.1    Hsieh, E.J.2    Watanabe, S.3    Allan, C.M.4    Chen, J.Y.5    Tran, U.C.6    Clarke, C.F.7
  • 36
    • 13244264954 scopus 로고    scopus 로고
    • Genetic evidence for a multi-subunit complex in coenzyme Q biosynthesis in yeast and the role of the Coq1 hexaprenyl diphosphate synthase
    • P. Gin, and C.F. Clarke Genetic evidence for a multi-subunit complex in coenzyme Q biosynthesis in yeast and the role of the Coq1 hexaprenyl diphosphate synthase J. Biol. Chem. 280 2005 2676 2681
    • (2005) J. Biol. Chem. , vol.280 , pp. 2676-2681
    • Gin, P.1    Clarke, C.F.2
  • 37
    • 30044432823 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae COQ10 gene encodes a START domain protein required for function of coenzyme Q in respiration
    • M.H. Barros, A. Johnson, P. Gin, B.N. Marbois, C.F. Clarke, and A. Tzagoloff The Saccharomyces cerevisiae COQ10 gene encodes a START domain protein required for function of coenzyme Q in respiration J. Biol. Chem. 280 2005 42627 42635
    • (2005) J. Biol. Chem. , vol.280 , pp. 42627-42635
    • Barros, M.H.1    Johnson, A.2    Gin, P.3    Marbois, B.N.4    Clarke, C.F.5    Tzagoloff, A.6
  • 38
  • 39
    • 58449099405 scopus 로고    scopus 로고
    • Coq10, a mitochondrial coenzyme Q binding protein, is required for proper respiration in Schizosaccharomyces pombe
    • T.Z. Cui, and M. Kawamukai Coq10, a mitochondrial coenzyme Q binding protein, is required for proper respiration in Schizosaccharomyces pombe FEBS J. 276 2009 748 759
    • (2009) FEBS J. , vol.276 , pp. 748-759
    • Cui, T.Z.1    Kawamukai, M.2
  • 40
    • 12944284529 scopus 로고    scopus 로고
    • NMR structure of the 18 kDa protein CC1736 from Caulobacter crescentus identifies a member of the START domain superfamily and suggests residues mediating substrate specificity
    • Y. Shen, S. Goldsmith-Fischman, H.S. Atreya, T. Acton, L. Ma, R. Xiao, B. Honig, G.T. Montelione, and T. Szyperski NMR structure of the 18 kDa protein CC1736 from Caulobacter crescentus identifies a member of the START domain superfamily and suggests residues mediating substrate specificity Proteins 58 2005 747 750
    • (2005) Proteins , vol.58 , pp. 747-750
    • Shen, Y.1    Goldsmith-Fischman, S.2    Atreya, H.S.3    Acton, T.4    Ma, L.5    Xiao, R.6    Honig, B.7    Montelione, G.T.8    Szyperski, T.9
  • 41
    • 84857854776 scopus 로고    scopus 로고
    • The mammalian START domain protein family in lipid transport in health and disease
    • B.J. Clark The mammalian START domain protein family in lipid transport in health and disease J. Endocrinol. 212 2012 257 275
    • (2012) J. Endocrinol. , vol.212 , pp. 257-275
    • Clark, B.J.1
  • 44
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • G. Christine, R.F. Gerald, Academic Press
    • R. Daniel Gietz, and R.A. Woods Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method G. Christine, R.F. Gerald, Methods Enzymol vol. 350 2002 Academic Press 87 96
    • (2002) Methods Enzymol , vol.350 , pp. 87-96
    • Daniel Gietz, R.1    Woods, R.A.2
  • 45
    • 0030988484 scopus 로고    scopus 로고
    • Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis
    • R.J. Barkovich, A. Shtanko, J.A. Shepherd, P.T. Lee, D.C. Myles, A. Tzagoloff, and C.F. Clarke Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis J. Biol. Chem. 272 1997 9182 9188
    • (1997) J. Biol. Chem. , vol.272 , pp. 9182-9188
    • Barkovich, R.J.1    Shtanko, A.2    Shepherd, J.A.3    Lee, P.T.4    Myles, D.C.5    Tzagoloff, A.6    Clarke, C.F.7
  • 46
    • 1842478452 scopus 로고    scopus 로고
    • A tRNATRP gene mediates the suppression of cbs2-223 previously attributed to ABC1/COQ8
    • E.J. Hsieh, J.B. Dinoso, and C.F. Clarke A tRNATRP gene mediates the suppression of cbs2-223 previously attributed to ABC1/COQ8 Biochem. Biophys. Res. Commun. 317 2004 648 653
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 648-653
    • Hsieh, E.J.1    Dinoso, J.B.2    Clarke, C.F.3
  • 47
    • 0025975314 scopus 로고
    • Analysis of mitochondrial function and assembly
    • M.P. Yaffe Analysis of mitochondrial function and assembly Methods Enzymol. 194 1991 627 643
    • (1991) Methods Enzymol. , vol.194 , pp. 627-643
    • Yaffe, M.P.1
  • 48
    • 0028800976 scopus 로고
    • Isolation of highly purified mitochondria from Saccharomyces cerevisiae
    • B.S. Glick, and L.A. Pon Isolation of highly purified mitochondria from Saccharomyces cerevisiae Methods Enzymol. 260 1995 213 223
    • (1995) Methods Enzymol. , vol.260 , pp. 213-223
    • Glick, B.S.1    Pon, L.A.2
  • 49
    • 0037816166 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-dependent monooxygenase required for coenzyme Q biosynthesis
    • P. Gin, A.Y. Hsu, S.C. Rothman, T. Jonassen, P.T. Lee, A. Tzagoloff, and C.F. Clarke The Saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-dependent monooxygenase required for coenzyme Q biosynthesis J. Biol. Chem. 278 2003 25308 25316
    • (2003) J. Biol. Chem. , vol.278 , pp. 25308-25316
    • Gin, P.1    Hsu, A.Y.2    Rothman, S.C.3    Jonassen, T.4    Lee, P.T.5    Tzagoloff, A.6    Clarke, C.F.7
  • 51
    • 0030016042 scopus 로고    scopus 로고
    • Mrs5p, an essential protein of the mitochondrial intermembrane space, affects protein import into yeast mitochondria
    • E. Jarosch, G. Tuller, G. Daum, M. Waldherr, A. Voskova, and R.J. Schweyen Mrs5p, an essential protein of the mitochondrial intermembrane space, affects protein import into yeast mitochondria J. Biol. Chem. 271 1996 17219 17225
    • (1996) J. Biol. Chem. , vol.271 , pp. 17219-17225
    • Jarosch, E.1    Tuller, G.2    Daum, G.3    Waldherr, M.4    Voskova, A.5    Schweyen, R.J.6
  • 52
    • 0026611680 scopus 로고
    • Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism
    • B.S. Glick, A. Brandt, K. Cunningham, S. Muller, R.L. Hallberg, and G. Schatz Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism Cell 69 1992 809 822
    • (1992) Cell , vol.69 , pp. 809-822
    • Glick, B.S.1    Brandt, A.2    Cunningham, K.3    Muller, S.4    Hallberg, R.L.5    Schatz, G.6
  • 53
    • 0037370059 scopus 로고    scopus 로고
    • Far3 and five interacting proteins prevent premature recovery from pheromone arrest in the budding yeast Saccharomyces cerevisiae
    • H.A. Kemp, and G.F. Sprague Jr. Far3 and five interacting proteins prevent premature recovery from pheromone arrest in the budding yeast Saccharomyces cerevisiae Mol. Cell. Biol. 23 2003 1750 1763
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1750-1763
    • Kemp, H.A.1    Sprague, Jr.G.F.2
  • 54
    • 0029081152 scopus 로고
    • Biogenesis of mitochondrial heme lyases in yeast. Import and folding in the intermembrane space
    • H. Steiner, A. Zollner, A. Haid, W. Neupert, and R. Lill Biogenesis of mitochondrial heme lyases in yeast. Import and folding in the intermembrane space J. Biol. Chem. 270 1995 22842 22849
    • (1995) J. Biol. Chem. , vol.270 , pp. 22842-22849
    • Steiner, H.1    Zollner, A.2    Haid, A.3    Neupert, W.4    Lill, R.5
  • 55
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondrial protein import in yeast
    • M.P. Yaffe, and G. Schatz Two nuclear mutations that block mitochondrial protein import in yeast Proc. Natl. Acad. Sci. U. S. A. 81 1984 4819 4823
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 4819-4823
    • Yaffe, M.P.1    Schatz, G.2
  • 56
    • 0033198845 scopus 로고    scopus 로고
    • Different import pathways through the mitochondrial intermembrane space for inner membrane proteins
    • D. Leuenberger, N.A. Bally, G. Schatz, and C.M. Koehler Different import pathways through the mitochondrial intermembrane space for inner membrane proteins EMBO J. 18 1999 4816 4822
    • (1999) EMBO J. , vol.18 , pp. 4816-4822
    • Leuenberger, D.1    Bally, N.A.2    Schatz, G.3    Koehler, C.M.4
  • 57
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Y. Fujiki, A.L. Hubbard, S. Fowler, and P.B. Lazarow Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum J. Cell Biol. 93 1982 97 102
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 58
    • 0024972079 scopus 로고
    • Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor
    • D.S. Reading, R.L. Hallberg, and A.M. Myers Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor Nature 337 1989 655 659
    • (1989) Nature , vol.337 , pp. 655-659
    • Reading, D.S.1    Hallberg, R.L.2    Myers, A.M.3
  • 59
    • 0023644921 scopus 로고
    • Phosphodiester bond cleavage outside mitochondria is required for the completion of protein import into the mitochondrial matrix
    • W.J. Chen, and M.G. Douglas Phosphodiester bond cleavage outside mitochondria is required for the completion of protein import into the mitochondrial matrix Cell 49 1987 651 658
    • (1987) Cell , vol.49 , pp. 651-658
    • Chen, W.J.1    Douglas, M.G.2
  • 60
    • 0020479711 scopus 로고
    • Import of proteins into mitochondria. The precursor of cytochrome c1 is processed in two steps, one of them heme-dependent
    • A. Ohashi, J. Gibson, I. Gregor, and G. Schatz Import of proteins into mitochondria. The precursor of cytochrome c1 is processed in two steps, one of them heme-dependent J. Biol. Chem. 257 1982 13042 13047
    • (1982) J. Biol. Chem. , vol.257 , pp. 13042-13047
    • Ohashi, A.1    Gibson, J.2    Gregor, I.3    Schatz, G.4
  • 61
    • 0035823556 scopus 로고    scopus 로고
    • A new member of the family of di-iron carboxylate proteins. Coq7 (clk-1), a membrane-bound hydroxylase involved in ubiquinone biosynthesis
    • P. Stenmark, J. Grunler, J. Mattsson, P.J. Sindelar, P. Nordlund, and D.A. Berthold A new member of the family of di-iron carboxylate proteins. Coq7 (clk-1), a membrane-bound hydroxylase involved in ubiquinone biosynthesis J. Biol. Chem. 276 2001 33297 33300
    • (2001) J. Biol. Chem. , vol.276 , pp. 33297-33300
    • Stenmark, P.1    Grunler, J.2    Mattsson, J.3    Sindelar, P.J.4    Nordlund, P.5    Berthold, D.A.6
  • 62
    • 0141661868 scopus 로고    scopus 로고
    • Membrane-bound diiron carboxylate proteins
    • D.A. Berthold, and P. Stenmark Membrane-bound diiron carboxylate proteins Annu. Rev. Plant Biol. 54 2003 497 517
    • (2003) Annu. Rev. Plant Biol. , vol.54 , pp. 497-517
    • Berthold, D.A.1    Stenmark, P.2
  • 63
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • D. Picot, P.J. Loll, and R.M. Garavito The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1 Nature 367 1994 243 249
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 64
    • 0033548169 scopus 로고    scopus 로고
    • The structure of the membrane protein squalene-hopene cyclase at 2.0 A resolution
    • K.U. Wendt, A. Lenhart, and G.E. Schulz The structure of the membrane protein squalene-hopene cyclase at 2.0 A resolution J. Mol. Biol. 286 1999 175 187
    • (1999) J. Mol. Biol. , vol.286 , pp. 175-187
    • Wendt, K.U.1    Lenhart, A.2    Schulz, G.E.3
  • 65
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction: Evidence for the extended lipid anchorage
    • E.K. Tuominen, C.J. Wallace, and P.K. Kinnunen Phospholipid-cytochrome c interaction: evidence for the extended lipid anchorage J. Biol. Chem. 277 2002 8822 8826
    • (2002) J. Biol. Chem. , vol.277 , pp. 8822-8826
    • Tuominen, E.K.1    Wallace, C.J.2    Kinnunen, P.K.3
  • 66
    • 1642391445 scopus 로고    scopus 로고
    • Yeast Coq5 C-methyltransferase is required for stability of other polypeptides involved in coenzyme Q biosynthesis
    • S.W. Baba, G.I. Belogrudov, J.C. Lee, P.T. Lee, J. Strahan, J.N. Shepherd, and C.F. Clarke Yeast Coq5 C-methyltransferase is required for stability of other polypeptides involved in coenzyme Q biosynthesis J. Biol. Chem. 279 2004 10052 10059
    • (2004) J. Biol. Chem. , vol.279 , pp. 10052-10059
    • Baba, S.W.1    Belogrudov, G.I.2    Lee, J.C.3    Lee, P.T.4    Strahan, J.5    Shepherd, J.N.6    Clarke, C.F.7
  • 68
    • 0033618376 scopus 로고    scopus 로고
    • Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis
    • W.W. Poon, R.J. Barkovich, A.Y. Hsu, A. Frankel, P.T. Lee, J.N. Shepherd, D.C. Myles, and C.F. Clarke Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis J. Biol. Chem. 274 1999 21665 21672
    • (1999) J. Biol. Chem. , vol.274 , pp. 21665-21672
    • Poon, W.W.1    Barkovich, R.J.2    Hsu, A.Y.3    Frankel, A.4    Lee, P.T.5    Shepherd, J.N.6    Myles, D.C.7    Clarke, C.F.8
  • 69
    • 20444392739 scopus 로고    scopus 로고
    • Interactions of mitochondria-targeted and untargeted ubiquinones with the mitochondrial respiratory chain and reactive oxygen species. Implications for the use of exogenous ubiquinones as therapies and experimental tools
    • A.M. James, H.M. Cocheme, R.A. Smith, and M.P. Murphy Interactions of mitochondria-targeted and untargeted ubiquinones with the mitochondrial respiratory chain and reactive oxygen species. Implications for the use of exogenous ubiquinones as therapies and experimental tools J. Biol. Chem. 280 2005 21295 21312
    • (2005) J. Biol. Chem. , vol.280 , pp. 21295-21312
    • James, A.M.1    Cocheme, H.M.2    Smith, R.A.3    Murphy, M.P.4
  • 70
    • 0037192846 scopus 로고    scopus 로고
    • Uptake of exogenous coenzyme Q and transport to mitochondria is required for bc1 complex stability in yeast coq mutants
    • C. Santos-Ocana, T.Q. Do, S. Padilla, P. Navas, and C.F. Clarke Uptake of exogenous coenzyme Q and transport to mitochondria is required for bc1 complex stability in yeast coq mutants J. Biol. Chem. 277 2002 10973 10981
    • (2002) J. Biol. Chem. , vol.277 , pp. 10973-10981
    • Santos-Ocana, C.1    Do, T.Q.2    Padilla, S.3    Navas, P.4    Clarke, C.F.5
  • 71
    • 77956235773 scopus 로고    scopus 로고
    • Bacteria, yeast, worms, and flies: Exploiting simple model organisms to investigate human mitochondrial diseases
    • S.L. Rea, B.H. Graham, E. Nakamaru-Ogiso, A. Kar, and M.J. Falk Bacteria, yeast, worms, and flies: exploiting simple model organisms to investigate human mitochondrial diseases Dev. Disabil. Res. Rev. 16 2010 200 218
    • (2010) Dev. Disabil. Res. Rev. , vol.16 , pp. 200-218
    • Rea, S.L.1    Graham, B.H.2    Nakamaru-Ogiso, E.3    Kar, A.4    Falk, M.J.5
  • 72
    • 67749089506 scopus 로고    scopus 로고
    • Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms
    • M. Kawamukai Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms Biotechnol. Appl. Biochem. 53 2009 217 226
    • (2009) Biotechnol. Appl. Biochem. , vol.53 , pp. 217-226
    • Kawamukai, M.1
  • 74
    • 0142025150 scopus 로고    scopus 로고
    • Fission yeast decaprenyl diphosphate synthase consists of Dps1 and the newly characterized Dlp1 protein in a novel heterotetrameric structure
    • R. Saiki, A. Nagata, N. Uchida, T. Kainou, H. Matsuda, and M. Kawamukai Fission yeast decaprenyl diphosphate synthase consists of Dps1 and the newly characterized Dlp1 protein in a novel heterotetrameric structure Eur. J. Biochem. 270 2003 4113 4121
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4113-4121
    • Saiki, R.1    Nagata, A.2    Uchida, N.3    Kainou, T.4    Matsuda, H.5    Kawamukai, M.6
  • 75
    • 27644497075 scopus 로고    scopus 로고
    • Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans
    • R. Saiki, A. Nagata, T. Kainou, H. Matsuda, and M. Kawamukai Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans FEBS J. 272 2005 5606 5622
    • (2005) FEBS J. , vol.272 , pp. 5606-5622
    • Saiki, R.1    Nagata, A.2    Kainou, T.3    Matsuda, H.4    Kawamukai, M.5
  • 80
    • 0034969390 scopus 로고    scopus 로고
    • Do sterols reduce proton and sodium leaks through lipid bilayers?
    • T.H. Haines Do sterols reduce proton and sodium leaks through lipid bilayers? Prog. Lipid Res. 40 2001 299 324
    • (2001) Prog. Lipid Res. , vol.40 , pp. 299-324
    • Haines, T.H.1
  • 81
    • 33646810851 scopus 로고    scopus 로고
    • Influence of the chain length of ubiquinones on their interaction with DPPC in mixed monolayers
    • Y. Roche, P. Peretti, and S. Bernard Influence of the chain length of ubiquinones on their interaction with DPPC in mixed monolayers Biochim. Biophys. Acta 1758 2006 468 478
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 468-478
    • Roche, Y.1    Peretti, P.2    Bernard, S.3
  • 83
    • 84895726388 scopus 로고    scopus 로고
    • Functional role of mitochondrial respiratory supercomplexes
    • (in press)
    • M.L. Genova, and G. Lenaz Functional role of mitochondrial respiratory supercomplexes Biochim. Biophys. Acta 2013 (in press)
    • (2013) Biochim. Biophys. Acta
    • Genova, M.L.1    Lenaz, G.2
  • 85
    • 77951233551 scopus 로고    scopus 로고
    • Complementation of coenzyme Q-deficient yeast by coenzyme Q analogues requires the isoprenoid side chain
    • A.M. James, H.M. Cocheme, M. Murai, H. Miyoshi, and M.P. Murphy Complementation of coenzyme Q-deficient yeast by coenzyme Q analogues requires the isoprenoid side chain FEBS J. 277 2010 2067 2082
    • (2010) FEBS J. , vol.277 , pp. 2067-2082
    • James, A.M.1    Cocheme, H.M.2    Murai, M.3    Miyoshi, H.4    Murphy, M.P.5
  • 87
    • 45949099527 scopus 로고    scopus 로고
    • Early coenzyme Q10 supplementation in primary coenzyme Q10 deficiency
    • G. Montini, C. Malaventura, and L. Salviati Early coenzyme Q10 supplementation in primary coenzyme Q10 deficiency N. Engl. J. Med. 358 2008 2849 2850
    • (2008) N. Engl. J. Med. , vol.358 , pp. 2849-2850
    • Montini, G.1    Malaventura, C.2    Salviati, L.3
  • 90
    • 84887565727 scopus 로고    scopus 로고
    • Mitochondrial respiration without ubiquinone biosynthesis
    • Y. Wang, and S. Hekimi Mitochondrial respiration without ubiquinone biosynthesis Hum. Mol. Genet. 22 2013 4768 4783
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 4768-4783
    • Wang, Y.1    Hekimi, S.2
  • 91
    • 0037160138 scopus 로고    scopus 로고
    • Development and fertility in Caenorhabditis elegans clk-1 mutants depend upon transport of dietary coenzyme Q8 to mitochondria
    • T. Jonassen, B.N. Marbois, K.F. Faull, C.F. Clarke, and P.L. Larsen Development and fertility in Caenorhabditis elegans clk-1 mutants depend upon transport of dietary coenzyme Q8 to mitochondria J. Biol. Chem. 277 2002 45020 45027
    • (2002) J. Biol. Chem. , vol.277 , pp. 45020-45027
    • Jonassen, T.1    Marbois, B.N.2    Faull, K.F.3    Clarke, C.F.4    Larsen, P.L.5
  • 92
    • 84864506396 scopus 로고    scopus 로고
    • Restoring de novo coenzyme Q biosynthesis in Caenorhabditis elegans coq-3 mutants yields profound rescue compared to exogenous coenzyme Q supplementation
    • F. Gomez, R. Saiki, R. Chin, C. Srinivasan, and C.F. Clarke Restoring de novo coenzyme Q biosynthesis in Caenorhabditis elegans coq-3 mutants yields profound rescue compared to exogenous coenzyme Q supplementation Gene 506 2012 106 116
    • (2012) Gene , vol.506 , pp. 106-116
    • Gomez, F.1    Saiki, R.2    Chin, R.3    Srinivasan, C.4    Clarke, C.F.5
  • 96
    • 0022976206 scopus 로고
    • Nuclear functions required for cytochrome c oxidase biogenesis in Saccharomyces cerevisiae. Characterization of mutants in 34 complementation groups
    • J.E. McEwen, C. Ko, B. Kloeckner-Gruissem, and R.O. Poyton Nuclear functions required for cytochrome c oxidase biogenesis in Saccharomyces cerevisiae. Characterization of mutants in 34 complementation groups J. Biol. Chem. 261 1986 11872 11879
    • (1986) J. Biol. Chem. , vol.261 , pp. 11872-11879
    • McEwen, J.E.1    Ko, C.2    Kloeckner-Gruissem, B.3    Poyton, R.O.4
  • 97
    • 0026731820 scopus 로고
    • COQ2 is a candidate for the structural gene encoding para- hydroxybenzoate:polyprenyltransferase
    • M.N. Ashby, S.Y. Kutsunai, S. Ackerman, A. Tzagoloff, and P.A. Edwards COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate: polyprenyltransferase J. Biol. Chem. 267 1992 4128 4136
    • (1992) J. Biol. Chem. , vol.267 , pp. 4128-4136
    • Ashby, M.N.1    Kutsunai, S.Y.2    Ackerman, S.3    Tzagoloff, A.4    Edwards, P.A.5
  • 98
    • 0029799910 scopus 로고    scopus 로고
    • Enhanced sensitivity of ubiquinone-deficient mutants of Saccharomyces cerevisiae to products of autoxidized polyunsaturated fatty acids
    • T.Q. Do, J.R. Schultz, and C.F. Clarke Enhanced sensitivity of ubiquinone-deficient mutants of Saccharomyces cerevisiae to products of autoxidized polyunsaturated fatty acids Proc. Natl. Acad. Sci. U. S. A. 93 1996 7534 7539
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7534-7539
    • Do, T.Q.1    Schultz, J.R.2    Clarke, C.F.3
  • 99
    • 0034630103 scopus 로고    scopus 로고
    • Genetic evidence for a multi-subunit complex in the O-methyltransferase steps of coenzyme Q biosynthesis
    • A.Y. Hsu, T.Q. Do, P.T. Lee, and C.F. Clarke Genetic evidence for a multi-subunit complex in the O-methyltransferase steps of coenzyme Q biosynthesis Biochim. Biophys. Acta 1484 2000 287 297
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 287-297
    • Hsu, A.Y.1    Do, T.Q.2    Lee, P.T.3    Clarke, C.F.4


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