메뉴 건너뛰기




Volumn 26, Issue 13, 2006, Pages 4872-4881

Cytochrome c oxidase is required for the assembly/stability of respiratory complex I in mouse fibroblasts

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOLIPIN; CYTOCHROME C OXIDASE; DNA; HEME; MITOCHONDRIAL DNA; NUCLEOTIDE; PROTEIN FARNESYLTRANSFERASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 33745478725     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01767-05     Document Type: Article
Times cited : (210)

References (36)
  • 3
    • 0142154270 scopus 로고    scopus 로고
    • Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency
    • Antonicka, H., S. C. Leary, G. H. Guercin, J. N. Agar, R. Horvath, N. G. Kennaway, C. O. Harding, M. Jaksch, and E. A. Shoubridge. 2003. Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency. Hum. Mol. Genet. 12:2693-2702.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2693-2702
    • Antonicka, H.1    Leary, S.C.2    Guercin, G.H.3    Agar, J.N.4    Horvath, R.5    Kennaway, N.G.6    Harding, C.O.7    Jaksch, M.8    Shoubridge, E.A.9
  • 4
    • 0033563018 scopus 로고    scopus 로고
    • Quantitation and origin of the mitochondrial membrane potential in human cells lacking mitochondrial DNA
    • Appleby, R. D., W. K. Porteous, G. Hughes, A. M. James, D. Shannon, Y. H. Wei, and M. P. Murphy. 1999. Quantitation and origin of the mitochondrial membrane potential in human cells lacking mitochondrial DNA. Eur. J. Biochem. 262:108-116.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 108-116
    • Appleby, R.D.1    Porteous, W.K.2    Hughes, G.3    James, A.M.4    Shannon, D.5    Wei, Y.H.6    Murphy, M.P.7
  • 5
    • 0032486399 scopus 로고    scopus 로고
    • Human xenomitochondrial cybrids. Cellular models of mitochondrial complex I deficiency
    • Barrientos, A., L. Kenyon, and C. T. Moraes. 1998. Human xenomitochondrial cybrids. Cellular models of mitochondrial complex I deficiency. J. Biol. Chem. 273:14210-14217.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14210-14217
    • Barrientos, A.1    Kenyon, L.2    Moraes, C.T.3
  • 6
    • 4644319049 scopus 로고    scopus 로고
    • Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae
    • Barrientos, A., A. Zambrano, and A. Tzagoloff. 2004. Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae. EMBO J. 23:3472-3482.
    • (2004) EMBO J. , vol.23 , pp. 3472-3482
    • Barrientos, A.1    Zambrano, A.2    Tzagoloff, A.3
  • 7
    • 0035831217 scopus 로고    scopus 로고
    • Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme O
    • Barros, M. H., C. G. Carlson, D. M. Glerum, and A. Tzagoloff. 2001. Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme O. FEBS Lett. 492:133-138.
    • (2001) FEBS Lett. , vol.492 , pp. 133-138
    • Barros, M.H.1    Carlson, C.G.2    Glerum, D.M.3    Tzagoloff, A.4
  • 8
    • 0037051889 scopus 로고    scopus 로고
    • Regulation of the heme A biosynthetic pathway in Saccharomyces cerevisiae
    • Barros, M. H., and A. Tzagoloff. 2002. Regulation of the heme A biosynthetic pathway in Saccharomyces cerevisiae. FEBS Lett. 516:119-123.
    • (2002) FEBS Lett. , vol.516 , pp. 119-123
    • Barros, M.H.1    Tzagoloff, A.2
  • 9
    • 4344561983 scopus 로고    scopus 로고
    • The mitochondrial respiratory chain is partially organized in a supercomplex assembly: Kinetic evidence using flux control analysis
    • Bianchi, C., M. L. Genova, G. Parenti Castelli, and G. Lenaz. 2004. The mitochondrial respiratory chain is partially organized in a supercomplex assembly: kinetic evidence using flux control analysis. J. Biol. Chem. 279:36562-36569.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36562-36569
    • Bianchi, C.1    Genova, M.L.2    Parenti Castelli, G.3    Lenaz, G.4
  • 10
    • 0036713124 scopus 로고    scopus 로고
    • Identification of novel hemes generated by heme A synthase: Evidence for two successive monooxygenase reactions
    • Brown, K. R., B. M. Allan, P. Do, and E. L. Hegg. 2002. Identification of novel hemes generated by heme A synthase: evidence for two successive monooxygenase reactions. Biochemistry 41:10906-10913.
    • (2002) Biochemistry , vol.41 , pp. 10906-10913
    • Brown, K.R.1    Allan, B.M.2    Do, P.3    Hegg, E.L.4
  • 11
    • 0029876984 scopus 로고    scopus 로고
    • In vivo labeling and analysis of human mitochondrial translation products
    • Chomyn, A. 1996. In vivo labeling and analysis of human mitochondrial translation products. Methods Enzymol. 264:197-211.
    • (1996) Methods Enzymol. , vol.264 , pp. 197-211
    • Chomyn, A.1
  • 13
    • 24944447977 scopus 로고    scopus 로고
    • Mice lacking COX10 in skeletal muscle recapitulate the phenotype of progressive mitochondrial myopathies associated with cytochrome c oxidase deficiency
    • Diaz, F., C. K. Thomas, S. Garcia, D. Hernandez, and C. T. Moraes. 2005. Mice lacking COX10 in skeletal muscle recapitulate the phenotype of progressive mitochondrial myopathies associated with cytochrome c oxidase deficiency. Hum. Mol. Genet. 14:2737-2748.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2737-2748
    • Diaz, F.1    Thomas, C.K.2    Garcia, S.3    Hernandez, D.4    Moraes, C.T.5
  • 14
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissues
    • Folch, J., M. Lees, and G. H. Sloane Stanley. 1957. A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226:497-509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3
  • 15
    • 5644225624 scopus 로고    scopus 로고
    • Cardiolipin biosynthesis and mitochondrial respiratory chain function are interdependent
    • Gohil, V. M., P. Hayes, S. Matsuyama, H. Schagger, M. Schlame, and M. L. Greenberg. 2004. Cardiolipin biosynthesis and mitochondrial respiratory chain function are interdependent. J. Biol. Chem. 279:42612-42618.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42612-42618
    • Gohil, V.M.1    Hayes, P.2    Matsuyama, S.3    Schagger, H.4    Schlame, M.5    Greenberg, M.L.6
  • 16
    • 0033927332 scopus 로고    scopus 로고
    • Nitrogen cavitation for cell disruption to obtain mitochondria from cultured cells
    • Gottlieb, R. A., and S. Adachi. 2000. Nitrogen cavitation for cell disruption to obtain mitochondria from cultured cells. Methods Enzymol. 322:213-221.
    • (2000) Methods Enzymol. , vol.322 , pp. 213-221
    • Gottlieb, R.A.1    Adachi, S.2
  • 17
    • 0029556979 scopus 로고
    • T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl- transferase gene by site-directed recombination
    • Hennet, T., F. K. Hagen, L. A. Tabak, and J. D. Marth. 1995. T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-transferase gene by site-directed recombination. Proc. Natl. Acad. Sci. USA 92:12070-12074.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12070-12074
    • Hennet, T.1    Hagen, F.K.2    Tabak, L.A.3    Marth, J.D.4
  • 18
    • 0034669552 scopus 로고    scopus 로고
    • Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis
    • Jung, C., C. M. Higgins, and Z. Xu. 2000. Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis. Anal. Biochem. 286:214-223.
    • (2000) Anal. Biochem. , vol.286 , pp. 214-223
    • Jung, C.1    Higgins, C.M.2    Xu, Z.3
  • 19
    • 0344563473 scopus 로고    scopus 로고
    • Expression of the E6 and E7 genes of human papillomavirus (HPV16) extends the life span of human myoblasts
    • Lochmuller, H., T. Johns, and E. A. Shoubridge. 1999. Expression of the E6 and E7 genes of human papillomavirus (HPV16) extends the life span of human myoblasts. Exp. Cell Res. 248:186-193.
    • (1999) Exp. Cell Res. , vol.248 , pp. 186-193
    • Lochmuller, H.1    Johns, T.2    Shoubridge, E.A.3
  • 20
    • 0028152645 scopus 로고
    • Biosynthesis and functional role of haem O and haem A
    • Mogi, T., K. Saiki, and Y. Anraku. 1994. Biosynthesis and functional role of haem O and haem A. Mol. Microbiol. 14:391-398.
    • (1994) Mol. Microbiol. , vol.14 , pp. 391-398
    • Mogi, T.1    Saiki, K.2    Anraku, Y.3
  • 21
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini, L., U. Blomer, P. Gallay, D. Ory, R. Mulligan, F. H. Gage, I. M. Verma, and D. Trono. 1996. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272:263-267.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5    Gage, F.H.6    Verma, I.M.7    Trono, D.8
  • 22
    • 0036024975 scopus 로고    scopus 로고
    • Blue native electrophoresis to study mitochondrial and other protein complexes
    • Nijtmans, L. G., N. S. Henderson, and I. J. Holt. 2002. Blue native electrophoresis to study mitochondrial and other protein complexes. Methods 26:327-334.
    • (2002) Methods , vol.26 , pp. 327-334
    • Nijtmans, L.G.1    Henderson, N.S.2    Holt, I.J.3
  • 23
    • 0017117629 scopus 로고
    • An improved two dimensional thin-layer chromatography system for the separation of phosphatidylglycerol and its derivatives
    • Poorthuis, B. J., P. J. Yazaki, and K. Y. Hosteller. 1976. An improved two dimensional thin-layer chromatography system for the separation of phosphatidylglycerol and its derivatives. J. Lipid Res. 17:433-437.
    • (1976) J. Lipid Res. , vol.17 , pp. 433-437
    • Poorthuis, B.J.1    Yazaki, P.J.2    Hosteller, K.Y.3
  • 24
    • 33745470064 scopus 로고    scopus 로고
    • The early stage of complex I assembly is linked with complex III and IV supercomplex
    • 10.9: [Online]
    • Rocher, C., W. Fan, E. Ruiz-Pesini, and D. C. Wallace. 2005. The early stage of complex I assembly is linked with complex III and IV supercomplex. Mitochondrial Physiol. 10.9:63-64. [Online.] http://www.mitophysiology .org/index.php?mip2005_abstracts.
    • (2005) Mitochondrial Physiol. , pp. 63-64
    • Rocher, C.1    Fan, W.2    Ruiz-Pesini, E.3    Wallace, D.C.4
  • 25
    • 33744951975 scopus 로고    scopus 로고
    • Architecture of active mammalian respiratory chain supercomplexes
    • 20 March, posting date. doi:10.1074/jbc .MS13525200. [Epub ahead of print]
    • Schafer, E., H. Seelert, N. H. Reifschneider, F. Krause, N. A. Dencher, and J. Vonck. 20 March 2006, posting date. Architecture of active mammalian respiratory chain supercomplexes. J. Biol. Chem. [Online] doi:10.1074/jbc .MS13525200. [Epub ahead of print.]
    • (2006) J. Biol. Chem. [Online]
    • Schafer, E.1    Seelert, H.2    Reifschneider, N.H.3    Krause, F.4    Dencher, N.A.5    Vonck, J.6
  • 26
    • 4344630010 scopus 로고    scopus 로고
    • Significance of respirasomes for the assembly/stability of human respiratory chain complex I
    • Schagger, H., R. de Coo, M. F. Bauer, S. Hofmann, C. Godinot, and U. Brandt. 2004. Significance of respirasomes for the assembly/stability of human respiratory chain complex I. J. Biol. Chem. 279:36349-36353.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36349-36353
    • Schagger, H.1    De Coo, R.2    Bauer, M.F.3    Hofmann, S.4    Godinot, C.5    Brandt, U.6
  • 27
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schagger, H., and K. Pfeiffer. 2000. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19:1777-1783.
    • (2000) EMBO J. , vol.19 , pp. 1777-1783
    • Schagger, H.1    Pfeiffer, K.2
  • 28
    • 1042278126 scopus 로고    scopus 로고
    • Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans
    • Stroh, A., O. Anderka, K. Pfeiffer, T. Yagi, M. Finel, B. Ludwig, and H. Schagger. 2004. Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans. J. Biol. Chem. 279:5000-5007.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5000-5007
    • Stroh, A.1    Anderka, O.2    Pfeiffer, K.3    Yagi, T.4    Finel, M.5    Ludwig, B.6    Schagger, H.7
  • 30
    • 1642382090 scopus 로고    scopus 로고
    • Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency
    • Ugalde, C., R. J. Janssen, L. P. van den Heuvel, J. A. Smeitink, and L. G. Nijtmans. 2004. Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency. Hum. Mol. Genet. 13:659-667.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 659-667
    • Ugalde, C.1    Janssen, R.J.2    Van Den Heuvel, L.P.3    Smeitink, J.A.4    Nijtmans, L.G.5
  • 31
    • 13644252982 scopus 로고    scopus 로고
    • Separation of yeast phospholipids using one-dimensional thin-layer chromatography
    • Vaden, D. L., V. M. Gohil, Z. Gu, and M. L. Greenberg. 2005. Separation of yeast phospholipids using one-dimensional thin-layer chromatography. Anal. Biochem. 338:162-164.
    • (2005) Anal. Biochem. , vol.338 , pp. 162-164
    • Vaden, D.L.1    Gohil, V.M.2    Gu, Z.3    Greenberg, M.L.4
  • 33
    • 1542290022 scopus 로고    scopus 로고
    • Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1
    • Williams, S. L., I. Valnot, P. Rustin, and J. W. Taanman. 2004. Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1. J. Biol. Chem. 279:7462-7469.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7462-7469
    • Williams, S.L.1    Valnot, I.2    Rustin, P.3    Taanman, J.W.4
  • 34
    • 0030805957 scopus 로고    scopus 로고
    • Beef heart cytochrome c oxidase
    • Yoshikawa, S. 1997. Beef heart cytochrome c oxidase. Curr. Opin. Struct. Biol. 7:574-579.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 574-579
    • Yoshikawa, S.1
  • 35
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochrome oxidase: Progress, problems and postulates
    • Zaslavsky, D., and R. B. Gennis. 2000. Proton pumping by cytochrome oxidase: progress, problems and postulates. Biochim. Biophys. Acta 1458:164-179.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavsky, D.1    Gennis, R.B.2
  • 36
    • 0030853263 scopus 로고    scopus 로고
    • Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels
    • Zerbetto, E., L. Vergani, and F. Dabbeni-Sala. 1997. Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels. Electrophoresis 18:2059-2064.
    • (1997) Electrophoresis , vol.18 , pp. 2059-2064
    • Zerbetto, E.1    Vergani, L.2    Dabbeni-Sala, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.