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Volumn 1793, Issue 11, 2009, Pages 1776-1786

Synthesis of cytochrome c oxidase subunit 1 is translationally downregulated in the absence of functional F1F0-ATP synthase

Author keywords

Cox1p translational regulation; Cytochrome c oxidase assembly; F1F0 ATPase; Mitochondria; Mitochondrial membrane potential

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CYTOCHROME C OXIDASE; MITOCHONDRIAL PROTEIN; OLIGOMYCIN; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 71749086467     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2009.09.002     Document Type: Article
Times cited : (40)

References (64)
  • 2
    • 33644686458 scopus 로고    scopus 로고
    • Function, structure, and biogenesis of mitochondrial ATP synthase
    • Ackerman S.H., and Tzagoloff A. Function, structure, and biogenesis of mitochondrial ATP synthase. Prog. Nucleic Acid Res. Mol. Biol. 80 (2005) 95-133
    • (2005) Prog. Nucleic Acid Res. Mol. Biol. , vol.80 , pp. 95-133
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 5
    • 34547117624 scopus 로고    scopus 로고
    • An assembled complex IV maintains the stability and activity of complex I in mammalian mitochondria
    • Li Y., D'Aurelio M., Deng J.H., Park J.S., Manfredi G., Hu P., Lu J., and Bai Y. An assembled complex IV maintains the stability and activity of complex I in mammalian mitochondria. J. Biol. Chem. 282 (2007) 17557-17562
    • (2007) J. Biol. Chem. , vol.282 , pp. 17557-17562
    • Li, Y.1    D'Aurelio, M.2    Deng, J.H.3    Park, J.S.4    Manfredi, G.5    Hu, P.6    Lu, J.7    Bai, Y.8
  • 6
    • 0038052926 scopus 로고    scopus 로고
    • Cytochrome oxidase assembly does not require catalytically active cytochrome C
    • Barrientos A., Pierre D., Lee J., and Tzagoloff A. Cytochrome oxidase assembly does not require catalytically active cytochrome C. J. Biol. Chem. 278 (2003) 8881-8887
    • (2003) J. Biol. Chem. , vol.278 , pp. 8881-8887
    • Barrientos, A.1    Pierre, D.2    Lee, J.3    Tzagoloff, A.4
  • 7
    • 63249108609 scopus 로고    scopus 로고
    • Lack of cytochrome c in mouse fibroblasts disrupts assembly/stability of respiratory complexes I and IV
    • Vempati U.D., Han X., and Moraes C.T. Lack of cytochrome c in mouse fibroblasts disrupts assembly/stability of respiratory complexes I and IV. J. Biol. Chem. 284 (2008) 4383-4391
    • (2008) J. Biol. Chem. , vol.284 , pp. 4383-4391
    • Vempati, U.D.1    Han, X.2    Moraes, C.T.3
  • 8
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DiMauro S., and Schon E.A. Mitochondrial respiratory-chain diseases. N. Engl. J. Med. 348 (2003) 2656-2668
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2656-2668
    • DiMauro, S.1    Schon, E.A.2
  • 12
    • 1942453308 scopus 로고    scopus 로고
    • The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants
    • Mattiazzi M., Vijayvergiya C., Gajewski C.D., DeVivo D.C., Lenaz G., Wiedmann M., and Manfredi G. The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants. Hum. Mol. Genet. 13 (2004) 869-879
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 869-879
    • Mattiazzi, M.1    Vijayvergiya, C.2    Gajewski, C.D.3    DeVivo, D.C.4    Lenaz, G.5    Wiedmann, M.6    Manfredi, G.7
  • 14
    • 0025350272 scopus 로고
    • Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase
    • Ackerman S.H., and Tzagoloff A. Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 4986-4990
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 4986-4990
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 16
    • 0024299839 scopus 로고
    • The definition of mitochondrial H+ ATPase assembly defects in mit- mutants of Saccharomyces cerevisiae with a monoclonal antibody to the enzyme complex as an assembly probe
    • Hadikusumo R.G., Meltzer S., Choo W.M., Jean-Francois M.J., Linnane A.W., and Marzuki S. The definition of mitochondrial H+ ATPase assembly defects in mit- mutants of Saccharomyces cerevisiae with a monoclonal antibody to the enzyme complex as an assembly probe. Biochim. Biophys. Acta 933 (1988) 212-222
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 212-222
    • Hadikusumo, R.G.1    Meltzer, S.2    Choo, W.M.3    Jean-Francois, M.J.4    Linnane, A.W.5    Marzuki, S.6
  • 17
    • 0024371971 scopus 로고
    • Mitochondrial H+-ATPase in mutants of Saccharomyces cerevisiae with defective subunit 8 of the enzyme complex
    • Marzuki S., Watkins L.C., and Choo W.M. Mitochondrial H+-ATPase in mutants of Saccharomyces cerevisiae with defective subunit 8 of the enzyme complex. Biochim. Biophys. Acta 975 (1989) 222-230
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 222-230
    • Marzuki, S.1    Watkins, L.C.2    Choo, W.M.3
  • 18
    • 0024447422 scopus 로고
    • The role of subunit 4, a nuclear-encoded protein of the F0 sector of yeast mitochondrial ATP synthase, in the assembly of the whole complex
    • Paul M.F., Velours J., Arselin de Chateaubodeau G., Aigle M., and Guerin B. The role of subunit 4, a nuclear-encoded protein of the F0 sector of yeast mitochondrial ATP synthase, in the assembly of the whole complex. Eur. J. Biochem. 185 (1989) 163-171
    • (1989) Eur. J. Biochem. , vol.185 , pp. 163-171
    • Paul, M.F.1    Velours, J.2    Arselin de Chateaubodeau, G.3    Aigle, M.4    Guerin, B.5
  • 19
    • 0030746112 scopus 로고    scopus 로고
    • The subunit f of mitochondrial yeast ATP synthase-characterization of the protein and disruption of the structural gene ATP17
    • Spannagel C., Vaillier J., Arselin G., Graves P.V., and Velours J. The subunit f of mitochondrial yeast ATP synthase-characterization of the protein and disruption of the structural gene ATP17. Eur. J. Biochem. 247 (1997) 1111-1117
    • (1997) Eur. J. Biochem. , vol.247 , pp. 1111-1117
    • Spannagel, C.1    Vaillier, J.2    Arselin, G.3    Graves, P.V.4    Velours, J.5
  • 20
    • 53249087822 scopus 로고    scopus 로고
    • Respiratory mutations lead to different pleiotropic effects on OXPHOS complexes in yeast and in human cells
    • Electronic publication 2008 Sep 3418
    • Marsy S., Frachon P., Dujardin G., Lombes A., and Lemaire C. Respiratory mutations lead to different pleiotropic effects on OXPHOS complexes in yeast and in human cells. FEBS Lett. 582 (2008) 3489-3493 Electronic publication 2008 Sep 3418
    • (2008) FEBS Lett. , vol.582 , pp. 3489-3493
    • Marsy, S.1    Frachon, P.2    Dujardin, G.3    Lombes, A.4    Lemaire, C.5
  • 21
    • 0034122608 scopus 로고    scopus 로고
    • Maintenance and integrity of the mitochondrial genome: a plethora of nuclear genes in the budding yeast
    • Contamine V., and Picard M. Maintenance and integrity of the mitochondrial genome: a plethora of nuclear genes in the budding yeast. Microbiol. Mol. Biol. Rev. 64 (2000) 281-315
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 281-315
    • Contamine, V.1    Picard, M.2
  • 22
    • 33745188484 scopus 로고    scopus 로고
    • A "petite obligate" mutant of Saccharomyces cerevisiae: functional mtDNA is lethal in cells lacking the delta subunit of mitochondrial F1-ATPase
    • Duvezin-Caubet S., Rak M., Lefebvre-Legendre L., Tetaud E., Bonnefoy N., and di Rago J.P. A "petite obligate" mutant of Saccharomyces cerevisiae: functional mtDNA is lethal in cells lacking the delta subunit of mitochondrial F1-ATPase. J. Biol. Chem. 281 (2006) 16305-16313
    • (2006) J. Biol. Chem. , vol.281 , pp. 16305-16313
    • Duvezin-Caubet, S.1    Rak, M.2    Lefebvre-Legendre, L.3    Tetaud, E.4    Bonnefoy, N.5    di Rago, J.P.6
  • 23
    • 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., Butler C.A., and Fox T.D. Expression of a recoded nuclear gene inserted into yeast mitochondrial DNA is limited by mRNA-specific translational activation. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 5253-5257
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5253-5257
    • Steele, D.F.1    Butler, C.A.2    Fox, T.D.3
  • 24
    • 34249722612 scopus 로고    scopus 로고
    • Yeast cells lacking the mitochondrial gene encoding the ATP synthase subunit 6 exhibit a selective loss of complex IV and unusual mitochondrial morphology
    • Rak M., Tetaud E., Godard F., Sagot I., Salin B., Duvezin-Caubet S., Slonimski P.P., Rytka J., and di Rago J.P. Yeast cells lacking the mitochondrial gene encoding the ATP synthase subunit 6 exhibit a selective loss of complex IV and unusual mitochondrial morphology. J. Biol. Chem. 282 (2007) 10853-10864
    • (2007) J. Biol. Chem. , vol.282 , pp. 10853-10864
    • Rak, M.1    Tetaud, E.2    Godard, F.3    Sagot, I.4    Salin, B.5    Duvezin-Caubet, S.6    Slonimski, P.P.7    Rytka, J.8    di Rago, J.P.9
  • 25
    • 67349139921 scopus 로고    scopus 로고
    • Biochemical consequences in yeast of the human mitochondrial DNA 8993T>C mutation in the ATPase6 gene found in NARP/MILS patients
    • Mar 6. [Electronic publication ahead of print]
    • Kucharczyk R., Rak M., and di Rago J.P. Biochemical consequences in yeast of the human mitochondrial DNA 8993T>C mutation in the ATPase6 gene found in NARP/MILS patients. Biochim Biophys Acta (2009) Mar 6. [Electronic publication ahead of print]
    • (2009) Biochim Biophys Acta
    • Kucharczyk, R.1    Rak, M.2    di Rago, J.P.3
  • 26
    • 0027459190 scopus 로고
    • ATP synthase of yeast mitochondria. Isolation and disruption of the ATP epsilon gene
    • Guelin E., Chevallier J., Rigoulet M., Guerin B., and Velours J. ATP synthase of yeast mitochondria. Isolation and disruption of the ATP epsilon gene. J. Biol. Chem. 268 (1993) 161-167
    • (1993) J. Biol. Chem. , vol.268 , pp. 161-167
    • Guelin, E.1    Chevallier, J.2    Rigoulet, M.3    Guerin, B.4    Velours, J.5
  • 27
    • 0345255615 scopus 로고    scopus 로고
    • The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit delta
    • Duvezin-Caubet S., Caron M., Giraud M.F., Velours J., and di Rago J.P. The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit delta. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 13235-13240
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13235-13240
    • Duvezin-Caubet, S.1    Caron, M.2    Giraud, M.F.3    Velours, J.4    di Rago, J.P.5
  • 28
    • 43749103377 scopus 로고    scopus 로고
    • The F1Fo-ATP synthase complex influences the assembly state of the cytochrome bc1-cytochrome oxidase supercomplex and its association with the TIM23 machinery
    • Saddar S., Dienhart M.K., and Stuart R.A. The F1Fo-ATP synthase complex influences the assembly state of the cytochrome bc1-cytochrome oxidase supercomplex and its association with the TIM23 machinery. J. Biol. Chem. 283 (2008) 6677-6686
    • (2008) J. Biol. Chem. , vol.283 , pp. 6677-6686
    • Saddar, S.1    Dienhart, M.K.2    Stuart, R.A.3
  • 29
    • 33744939757 scopus 로고    scopus 로고
    • Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes
    • Bornhovd C., Vogel F., Neupert W., and Reichert A.S. Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes. J. Biol. Chem. 281 (2006) 13990-13998
    • (2006) J. Biol. Chem. , vol.281 , pp. 13990-13998
    • Bornhovd, C.1    Vogel, F.2    Neupert, W.3    Reichert, A.S.4
  • 30
    • 56149104649 scopus 로고    scopus 로고
    • Cytochrome c oxidase biogenesis: new levels of regulation
    • Fontanesi F., Soto I.C., and Barrientos A. Cytochrome c oxidase biogenesis: new levels of regulation. IUBMB Life 60 (2008) 557-568
    • (2008) IUBMB Life , vol.60 , pp. 557-568
    • Fontanesi, F.1    Soto, I.C.2    Barrientos, A.3
  • 31
    • 0025357629 scopus 로고
    • ATP10, a yeast nuclear gene required for the assembly of the mitochondrial F1-F0 complex
    • Ackerman S.H., and Tzagoloff A. ATP10, a yeast nuclear gene required for the assembly of the mitochondrial F1-F0 complex. J. Biol. Chem. 265 (1990) 9952-9959
    • (1990) J. Biol. Chem. , vol.265 , pp. 9952-9959
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 32
    • 4644319049 scopus 로고    scopus 로고
    • Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae
    • Barrientos A., Zambrano A., and Tzagoloff A. Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae. EMBO J. 23 (2004) 3472-3482
    • (2004) EMBO J. , vol.23 , pp. 3472-3482
    • Barrientos, A.1    Zambrano, A.2    Tzagoloff, A.3
  • 33
    • 0030802910 scopus 로고    scopus 로고
    • COX15 codes for a mitochondrial protein essential for the assembly of yeast cytochrome oxidase
    • Glerum D.M., Muroff I., Jin C., and Tzagoloff A. COX15 codes for a mitochondrial protein essential for the assembly of yeast cytochrome oxidase. J. Biol. Chem. 272 (1997) 19088-19094
    • (1997) J. Biol. Chem. , vol.272 , pp. 19088-19094
    • Glerum, D.M.1    Muroff, I.2    Jin, C.3    Tzagoloff, A.4
  • 34
    • 0022110054 scopus 로고
    • Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae
    • Myers A.M., Pape L.K., and Tzagoloff A. Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae. EMBO J. 4 (1985) 2087-2092
    • (1985) EMBO J. , vol.4 , pp. 2087-2092
    • Myers, A.M.1    Pape, L.K.2    Tzagoloff, A.3
  • 35
    • 0016270218 scopus 로고
    • Physical and genetic organization of petite and grande yeast mitochondrial DNA. IV. In vivo transcription products of mitochondrial DNA and localization of 23 S ribosomal RNA in petite mutants of Saccharomyces cerevisiae
    • Faye G., Kujawa C., and Fukuhara H. Physical and genetic organization of petite and grande yeast mitochondrial DNA. IV. In vivo transcription products of mitochondrial DNA and localization of 23 S ribosomal RNA in petite mutants of Saccharomyces cerevisiae. J. Mol. Biol. 88 (1974) 185-203
    • (1974) J. Mol. Biol. , vol.88 , pp. 185-203
    • Faye, G.1    Kujawa, C.2    Fukuhara, H.3
  • 36
    • 0037080769 scopus 로고    scopus 로고
    • Shy1p is necessary for full expression of mitochondrial COX1 in the yeast model of Leigh's syndrome
    • Barrientos A., Korr D., and Tzagoloff A. Shy1p is necessary for full expression of mitochondrial COX1 in the yeast model of Leigh's syndrome. EMBO J. 21 (2002) 43-52
    • (2002) EMBO J. , vol.21 , pp. 43-52
    • Barrientos, A.1    Korr, D.2    Tzagoloff, A.3
  • 37
    • 0000970212 scopus 로고
    • The colorimetric determination of phosphorus
    • King E.J. The colorimetric determination of phosphorus. Biochem. J. 26 (1932) 292-297
    • (1932) Biochem. J. , vol.26 , pp. 292-297
    • King, E.J.1
  • 38
    • 0035215775 scopus 로고    scopus 로고
    • Assessment of mitochondrial membrane potential in yeast cell populations by flow cytometry
    • Ludovico P., Sansonetty F., and Corte-Real M. Assessment of mitochondrial membrane potential in yeast cell populations by flow cytometry. Microbiology 147 (2001) 3335-3343
    • (2001) Microbiology , vol.147 , pp. 3335-3343
    • Ludovico, P.1    Sansonetty, F.2    Corte-Real, M.3
  • 39
    • 0034176843 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and neuronal glutamate excitotoxicity: mortality and millivolts
    • Nicholls D.G., and Ward M.W. Mitochondrial membrane potential and neuronal glutamate excitotoxicity: mortality and millivolts. Trends Neurosci. 23 (2000) 166-174
    • (2000) Trends Neurosci. , vol.23 , pp. 166-174
    • Nicholls, D.G.1    Ward, M.W.2
  • 41
    • 40549085695 scopus 로고    scopus 로고
    • Transcriptional activators HAP/NF-Y rescue a cytochrome c oxidase defect in yeast and human cells
    • Fontanesi F., Jin C., Tzagoloff A., and Barrientos A. Transcriptional activators HAP/NF-Y rescue a cytochrome c oxidase defect in yeast and human cells. Hum. Mol. Genet. 17 (2008) 775-788
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 775-788
    • Fontanesi, F.1    Jin, C.2    Tzagoloff, A.3    Barrientos, A.4
  • 43
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl R.H., and Gietz R.D. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16 (1989) 339-346
    • (1989) Curr. Genet. , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 44
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein R.J. One-step gene disruption in yeast. Methods Enzymol. 101 (1983) 202-211
    • (1983) Methods Enzymol. , vol.101 , pp. 202-211
    • Rothstein, R.J.1
  • 46
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
    • 24044525272 scopus 로고    scopus 로고
    • Failure to assemble the alpha 3 beta 3 subcomplex of the ATP synthase leads to accumulation of the alpha and beta subunits within inclusion bodies and the loss of mitochondrial cristae in Saccharomyces cerevisiae
    • Lefebvre-Legendre L., Salin B., Schaeffer J., Brethes D., Dautant A., Ackerman S.H., and di Rago J.P. Failure to assemble the alpha 3 beta 3 subcomplex of the ATP synthase leads to accumulation of the alpha and beta subunits within inclusion bodies and the loss of mitochondrial cristae in Saccharomyces cerevisiae. J. Biol. Chem. 280 (2005) 18386-18392
    • (2005) J. Biol. Chem. , vol.280 , pp. 18386-18392
    • Lefebvre-Legendre, L.1    Salin, B.2    Schaeffer, J.3    Brethes, D.4    Dautant, A.5    Ackerman, S.H.6    di Rago, J.P.7
  • 49
    • 25844448754 scopus 로고    scopus 로고
    • Analysis of COX2 mutants reveals cytochrome oxidase subassemblies in yeast
    • Horan S., Bourges I., Taanman J.W., and Meunier B. Analysis of COX2 mutants reveals cytochrome oxidase subassemblies in yeast. Biochem J 390 (2005) 703-708
    • (2005) Biochem J , vol.390 , pp. 703-708
    • Horan, S.1    Bourges, I.2    Taanman, J.W.3    Meunier, B.4
  • 51
    • 0242473137 scopus 로고    scopus 로고
    • Mss51p promotes mitochondrial Cox1p synthesis and interacts with newly synthesized Cox1p
    • Perez-Martinez X., Broadley S.A., and Fox T.D. Mss51p promotes mitochondrial Cox1p synthesis and interacts with newly synthesized Cox1p. EMBO J. 22 (2003) 5951-5961
    • (2003) EMBO J. , vol.22 , pp. 5951-5961
    • Perez-Martinez, X.1    Broadley, S.A.2    Fox, T.D.3
  • 52
    • 33846794444 scopus 로고    scopus 로고
    • Aberrant translation of cytochrome c oxidase subunit 1 mRNA species in the absence of Mss51p in the yeast Saccharomyces cerevisiae
    • Zambrano A., Fontanesi F., Solans A., de Oliveira R.L., Fox T.D., Tzagoloff A., and Barrientos A. Aberrant translation of cytochrome c oxidase subunit 1 mRNA species in the absence of Mss51p in the yeast Saccharomyces cerevisiae. Mol. Biol. Cell 18 (2007) 523-535
    • (2007) Mol. Biol. Cell , vol.18 , pp. 523-535
    • Zambrano, A.1    Fontanesi, F.2    Solans, A.3    de Oliveira, R.L.4    Fox, T.D.5    Tzagoloff, A.6    Barrientos, A.7
  • 53
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences
    • Martin J., Mahlke K., and Pfanner N. Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences. J. Biol. Chem. 266 (1991) 18051-18057
    • (1991) J. Biol. Chem. , vol.266 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, N.3
  • 54
    • 0033739682 scopus 로고    scopus 로고
    • Membrane potential-driven protein import into mitochondria. The sorting sequence of cytochrome b(2) modulates the deltapsi-dependence of translocation of the matrix-targeting sequence
    • Geissler A., Krimmer T., Bomer U., Guiard B., Rassow J., and Pfanner N. Membrane potential-driven protein import into mitochondria. The sorting sequence of cytochrome b(2) modulates the deltapsi-dependence of translocation of the matrix-targeting sequence. Mol. Biol. Cell 11 (2000) 3977-3991
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3977-3991
    • Geissler, A.1    Krimmer, T.2    Bomer, U.3    Guiard, B.4    Rassow, J.5    Pfanner, N.6
  • 55
    • 0025781386 scopus 로고
    • Characterization of ATP12, a yeast nuclear gene required for the assembly of the mitochondrial F1-ATPase
    • Bowman S., Ackerman S.H., Griffiths D.E., and Tzagoloff A. Characterization of ATP12, a yeast nuclear gene required for the assembly of the mitochondrial F1-ATPase. J. Biol. Chem. 266 (1991) 7517-7523
    • (1991) J. Biol. Chem. , vol.266 , pp. 7517-7523
    • Bowman, S.1    Ackerman, S.H.2    Griffiths, D.E.3    Tzagoloff, A.4
  • 56
    • 0034599489 scopus 로고    scopus 로고
    • The alpha-subunit of the mitochondrial F(1) ATPase interacts directly with the assembly factor Atp12p
    • Wang Z.G., Sheluho D., Gatti D.L., and Ackerman S.H. The alpha-subunit of the mitochondrial F(1) ATPase interacts directly with the assembly factor Atp12p. EMBO J. 19 (2000) 1486-1493
    • (2000) EMBO J. , vol.19 , pp. 1486-1493
    • Wang, Z.G.1    Sheluho, D.2    Gatti, D.L.3    Ackerman, S.H.4
  • 57
    • 33845298268 scopus 로고    scopus 로고
    • Assembly of mitochondrial cytochrome c oxidase, a complicated and highly regulated cellular process
    • Fontanesi F., Soto I.C., Horn D., and Barrientos A. Assembly of mitochondrial cytochrome c oxidase, a complicated and highly regulated cellular process. Am. J. Physiol. Cell Physiol. 291 (2006) C1129-1147
    • (2006) Am. J. Physiol. Cell Physiol. , vol.291
    • Fontanesi, F.1    Soto, I.C.2    Horn, D.3    Barrientos, A.4
  • 58
    • 33846038738 scopus 로고    scopus 로고
    • Interaction between cytochrome caa3 and F1F0-ATP synthase of alkaliphilic Bacillus pseudofirmus OF4 is demonstrated by saturation transfer electron paramagnetic resonance and differential scanning calorimetry assays
    • Liu X., Gong X., Hicks D.B., Krulwich T.A., Yu L., and Yu C.A. Interaction between cytochrome caa3 and F1F0-ATP synthase of alkaliphilic Bacillus pseudofirmus OF4 is demonstrated by saturation transfer electron paramagnetic resonance and differential scanning calorimetry assays. Biochemistry 46 (2007) 306-313
    • (2007) Biochemistry , vol.46 , pp. 306-313
    • Liu, X.1    Gong, X.2    Hicks, D.B.3    Krulwich, T.A.4    Yu, L.5    Yu, C.A.6
  • 60
    • 0038070570 scopus 로고    scopus 로고
    • The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane
    • Arselin G., Giraud M.F., Dautant A., Vaillier J., Brethes D., Coulary-Salin B., Schaeffer J., and Velours J. The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane. Eur. J. Biochem. 270 (2003) 1875-1884
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1875-1884
    • Arselin, G.1    Giraud, M.F.2    Dautant, A.3    Vaillier, J.4    Brethes, D.5    Coulary-Salin, B.6    Schaeffer, J.7    Velours, J.8
  • 62
    • 0032534790 scopus 로고    scopus 로고
    • Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits
    • Arnold I., Pfeiffer K., Neupert W., Stuart R.A., and Schagger H. Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits. EMBO J. 17 (1998) 7170-7178
    • (1998) EMBO J. , vol.17 , pp. 7170-7178
    • Arnold, I.1    Pfeiffer, K.2    Neupert, W.3    Stuart, R.A.4    Schagger, H.5
  • 63
    • 34447338862 scopus 로고    scopus 로고
    • PGC-1alpha/beta upregulation is associated with improved oxidative phosphorylation in cells harboring nonsense mtDNA mutations
    • Srivastava S., Barrett J.N., and Moraes C.T. PGC-1alpha/beta upregulation is associated with improved oxidative phosphorylation in cells harboring nonsense mtDNA mutations. Hum. Mol. Genet. 16 (2007) 993-1005
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 993-1005
    • Srivastava, S.1    Barrett, J.N.2    Moraes, C.T.3
  • 64
    • 50049118173 scopus 로고    scopus 로고
    • Activation of the PPAR/PGC-1alpha pathway prevents a bioenergetic deficit and effectively improves a mitochondrial myopathy phenotype
    • Wenz T., Diaz F., Spiegelman B.M., and Moraes C.T. Activation of the PPAR/PGC-1alpha pathway prevents a bioenergetic deficit and effectively improves a mitochondrial myopathy phenotype. Cell Metab. 8 (2008) 249-256
    • (2008) Cell Metab. , vol.8 , pp. 249-256
    • Wenz, T.1    Diaz, F.2    Spiegelman, B.M.3    Moraes, C.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.