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Volumn 364, Issue 2, 2007, Pages 128-137

Analysis of mitochondrial subunit assembly into respiratory chain complexes using Blue Native polyacrylamide gel electrophoresis

Author keywords

Blue native PAGE; Membrane protein; Mitochondria; OXPHOS; Supercomplex

Indexed keywords

CELL CULTURE; DEFECTS; DIAGNOSIS; DNA; ELECTROPHORESIS; PROTEINS; SYNTHESIS (CHEMICAL);

EID: 34147153222     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.02.022     Document Type: Article
Times cited : (87)

References (38)
  • 1
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace D.C. Mitochondrial diseases in man and mouse. Science 283 (1999) 1482-1488
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 2
    • 0037009108 scopus 로고    scopus 로고
    • Import and assembly of proteins into mitochondria of mammalian cells
    • Hoogenraad N.J., Ward L.A., and Ryan M.T. Import and assembly of proteins into mitochondria of mammalian cells. Biochim. Biophys. Acta 1592 (2002) 97-105
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 97-105
    • Hoogenraad, N.J.1    Ward, L.A.2    Ryan, M.T.3
  • 3
    • 0021866528 scopus 로고
    • Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase
    • Chomyn A., Mariottini P., Cleeter M.W., Ragan C.I., Matsuno-Yagi A., Hatefi Y., Doolittle R.F., and Attardi G. Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature 314 (1985) 592-597
    • (1985) Nature , vol.314 , pp. 592-597
    • Chomyn, A.1    Mariottini, P.2    Cleeter, M.W.3    Ragan, C.I.4    Matsuno-Yagi, A.5    Hatefi, Y.6    Doolittle, R.F.7    Attardi, G.8
  • 4
    • 0023032242 scopus 로고
    • URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit
    • Chomyn A., Cleeter M.W., Ragan C.I., Riley M., Doolittle R.F., and Attardi G. URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit. Science 234 (1986) 614-618
    • (1986) Science , vol.234 , pp. 614-618
    • Chomyn, A.1    Cleeter, M.W.2    Ragan, C.I.3    Riley, M.4    Doolittle, R.F.5    Attardi, G.6
  • 5
    • 0029059067 scopus 로고
    • MtDNA mutation in MERRF syndrome causes defective aminoacylation of tRNA(Lys) and premature translation termination
    • Enriquez J.A., Chomyn A., and Attardi G. MtDNA mutation in MERRF syndrome causes defective aminoacylation of tRNA(Lys) and premature translation termination. Nat. Genet. 10 (1995) 47-55
    • (1995) Nat. Genet. , vol.10 , pp. 47-55
    • Enriquez, J.A.1    Chomyn, A.2    Attardi, G.3
  • 6
    • 0026573082 scopus 로고
    • Defects in mitochondrial protein synthesis and respiratory chain activity segregate with the tRNA(Leu(UUR)) mutation associated with mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes
    • King M.P., Koga Y., Davidson M., and Schon E.A. Defects in mitochondrial protein synthesis and respiratory chain activity segregate with the tRNA(Leu(UUR)) mutation associated with mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes. Mol. Cell Biol. 12 (1992) 480-490
    • (1992) Mol. Cell Biol. , vol.12 , pp. 480-490
    • King, M.P.1    Koga, Y.2    Davidson, M.3    Schon, E.A.4
  • 7
    • 0027270863 scopus 로고
    • Lack of assembly of mitochondrial DNA-encoded subunits of respiratory NADH dehydrogenase and loss of enzyme activity in a human cell mutant lacking the mitochondrial ND4 gene product
    • Hofhaus G., and Attardi G. Lack of assembly of mitochondrial DNA-encoded subunits of respiratory NADH dehydrogenase and loss of enzyme activity in a human cell mutant lacking the mitochondrial ND4 gene product. EMBO J. 12 (1993) 3043-3048
    • (1993) EMBO J. , vol.12 , pp. 3043-3048
    • Hofhaus, G.1    Attardi, G.2
  • 8
    • 0028889974 scopus 로고
    • Efficient selection and characterization of mutants of a human cell line which are defective in mitochondrial DNA-encoded subunits of respiratory NADH dehydrogenase
    • Hofhaus G., and Attardi G. Efficient selection and characterization of mutants of a human cell line which are defective in mitochondrial DNA-encoded subunits of respiratory NADH dehydrogenase. Mol. Cell. Biol. 15 (1995) 964-974
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 964-974
    • Hofhaus, G.1    Attardi, G.2
  • 9
    • 0026409298 scopus 로고
    • Blue Native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H., and von Jagow G. Blue Native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199 (1991) 223-231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 10
    • 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., Janssen R.J., van den Heuvel L.P., Smeitink J.A., and Nijtmans L.G. Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency. Hum. Mol. Genet. 13 (2004) 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
  • 11
    • 19544369483 scopus 로고    scopus 로고
    • Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: A framework to interpret complex I deficiencies
    • Ugalde C., Vogel R., Huijbens R., Van den Heuvel B., Smeitink J., and Nijtmans L. Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: A framework to interpret complex I deficiencies. Hum. Mol. Genet. 13 (2004) 2461-2472
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2461-2472
    • Ugalde, C.1    Vogel, R.2    Huijbens, R.3    Van den Heuvel, B.4    Smeitink, J.5    Nijtmans, L.6
  • 12
    • 0242353332 scopus 로고    scopus 로고
    • Identification and characterization of a common set of complex I assembly intermediates in mitochondria from patients with complex I deficiency
    • Antonicka H., Ogilvie I., Taivassalo T., Anitori R.P., Haller R.G., Vissing J., Kennaway N.G., and Shoubridge E.A. Identification and characterization of a common set of complex I assembly intermediates in mitochondria from patients with complex I deficiency. J. Biol. Chem. 278 (2003) 43081-43088
    • (2003) J. Biol. Chem. , vol.278 , pp. 43081-43088
    • Antonicka, H.1    Ogilvie, I.2    Taivassalo, T.3    Anitori, R.P.4    Haller, R.G.5    Vissing, J.6    Kennaway, N.G.7    Shoubridge, E.A.8
  • 14
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schagger H., and Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19 (2000) 1777-1783
    • (2000) EMBO J. , vol.19 , pp. 1777-1783
    • Schagger, H.1    Pfeiffer, K.2
  • 16
    • 0036139981 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes
    • Schagger H. Respiratory chain supercomplexes. IUBMB Life 52 (2001) 119-128
    • (2001) IUBMB Life , vol.52 , pp. 119-128
    • Schagger, H.1
  • 18
    • 4344630010 scopus 로고    scopus 로고
    • Significance of respirasomes for the assembly/stability of human respiratory chain complex I
    • Schagger H., de Coo R., Bauer M.F., Hofmann S., Godinot C., and Brandt U. Significance of respirasomes for the assembly/stability of human respiratory chain complex I. J. Biol. Chem. 279 (2004) 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
  • 19
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients
    • McKenzie M., Lazarou M., Thorburn D.R., and Ryan M.T. Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients. J. Mol. Biol. 361 (2006) 462-469
    • (2006) J. Mol. Biol. , vol.361 , pp. 462-469
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 20
    • 0032893995 scopus 로고    scopus 로고
    • Respiratory chain complex I deficiency: An underdiagnosed energy generation disorder
    • Kirby D.M., Crawford M., Cleary M.A., Dahl H.H., Dennett X., and Thorburn D.R. Respiratory chain complex I deficiency: An underdiagnosed energy generation disorder. Neurology 52 (1999) 1255-1264
    • (1999) Neurology , vol.52 , pp. 1255-1264
    • Kirby, D.M.1    Crawford, M.2    Cleary, M.A.3    Dahl, H.H.4    Dennett, X.5    Thorburn, D.R.6
  • 21
    • 0029876984 scopus 로고    scopus 로고
    • In vivo labeling and analysis of human mitochondrial translation products
    • Chomyn A. In vivo labeling and analysis of human mitochondrial translation products. Methods Enzymol. 264 (1996) 197-211
    • (1996) Methods Enzymol. , vol.264 , pp. 197-211
    • Chomyn, A.1
  • 22
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 24
    • 0017351588 scopus 로고
    • Metabolic properties of the products of mitochondrial protein synthesis in HeLa cells
    • Costantino P., and Attardi G. Metabolic properties of the products of mitochondrial protein synthesis in HeLa cells. J. Biol. Chem. 252 (1977) 1702-1711
    • (1977) J. Biol. Chem. , vol.252 , pp. 1702-1711
    • Costantino, P.1    Attardi, G.2
  • 25
    • 0037077251 scopus 로고    scopus 로고
    • Species-specific and mutant MWFE proteins: Their effect on the assembly of a functional mammalian mitochondrial complex I
    • Yadava N., Potluri P., Smith E.N., Bisevac A., and Scheffler I.E. Species-specific and mutant MWFE proteins: Their effect on the assembly of a functional mammalian mitochondrial complex I. J. Biol. Chem. 277 (2002) 21221-21230
    • (2002) J. Biol. Chem. , vol.277 , pp. 21221-21230
    • Yadava, N.1    Potluri, P.2    Smith, E.N.3    Bisevac, A.4    Scheffler, I.E.5
  • 26
    • 26444488636 scopus 로고    scopus 로고
    • A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy
    • Ogilvie I., Kennaway N.G., and Shoubridge E.A. A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy. J. Clin. Invest. 115 (2005) 2784-2792
    • (2005) J. Clin. Invest. , vol.115 , pp. 2784-2792
    • Ogilvie, I.1    Kennaway, N.G.2    Shoubridge, E.A.3
  • 28
    • 23844444516 scopus 로고    scopus 로고
    • 1 complex assembly in Saccharomyces cerevisiae
    • 1 complex assembly in Saccharomyces cerevisiae. Curr. Genet. 47 (2005) 203-212
    • (2005) Curr. Genet. , vol.47 , pp. 203-212
    • Kronekova, Z.1    Rodel, G.2
  • 29
    • 1642404614 scopus 로고    scopus 로고
    • 1 complex based on analysis of single and double deletion mutants lacking supernumerary subunits and cytochrome b
    • 1 complex based on analysis of single and double deletion mutants lacking supernumerary subunits and cytochrome b. Eur. J. Biochem. 271 (2004) 1209-1218
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1209-1218
    • Zara, V.1    Palmisano, I.2    Conte, L.3    Trumpower, B.L.4
  • 30
    • 0023726382 scopus 로고
    • Assembly of the mitochondrial membrane system: Analysis of structural mutants of the yeast coenzyme QH2-cytochrome c reductase complex
    • Crivellone M.D., Wu M.A., and Tzagoloff A. Assembly of the mitochondrial membrane system: Analysis of structural mutants of the yeast coenzyme QH2-cytochrome c reductase complex. J. Biol. Chem. 263 (1988) 14323-14333
    • (1988) J. Biol. Chem. , vol.263 , pp. 14323-14333
    • Crivellone, M.D.1    Wu, M.A.2    Tzagoloff, A.3
  • 31
    • 0034951707 scopus 로고    scopus 로고
    • Cytochrome c oxidase deficiency
    • Shoubridge E.A. Cytochrome c oxidase deficiency. Am. J. Med. Genet. 106 (2001) 46-52
    • (2001) Am. J. Med. Genet. , vol.106 , pp. 46-52
    • Shoubridge, E.A.1
  • 32
    • 0035851099 scopus 로고    scopus 로고
    • The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes
    • Schagger H., and Pfeiffer K. The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes. J. Biol. Chem. 276 (2001) 37861-37867
    • (2001) J. Biol. Chem. , vol.276 , pp. 37861-37867
    • Schagger, H.1    Pfeiffer, K.2
  • 33
    • 0029560518 scopus 로고
    • Assembly of mitochondrial ATP synthase in cultured human cells: Implications for mitochondrial diseases
    • Nijtmans L.G., Klement P., Houstek J., and van den Bogert C. Assembly of mitochondrial ATP synthase in cultured human cells: Implications for mitochondrial diseases. Biochim. Biophys. Acta 1272 (1995) 190-198
    • (1995) Biochim. Biophys. Acta , vol.1272 , pp. 190-198
    • Nijtmans, L.G.1    Klement, P.2    Houstek, J.3    van den Bogert, C.4
  • 34
    • 0036906870 scopus 로고    scopus 로고
    • Large functional range of steady-state levels of nuclear and mitochondrial transcripts coding for the subunits of the human mitochondrial OXPHOS system
    • Duborjal H., Beugnot R., De Camaret B.M., and Issartel J.P. Large functional range of steady-state levels of nuclear and mitochondrial transcripts coding for the subunits of the human mitochondrial OXPHOS system. Genome Res. 12 (2002) 1901-1909
    • (2002) Genome Res. , vol.12 , pp. 1901-1909
    • Duborjal, H.1    Beugnot, R.2    De Camaret, B.M.3    Issartel, J.P.4
  • 35
    • 0032541401 scopus 로고    scopus 로고
    • The mtDNA-encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and the respiratory function of the enzyme
    • Bai Y., and Attardi G. The mtDNA-encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and the respiratory function of the enzyme. EMBO J. 17 (1998) 4848-4858
    • (1998) EMBO J. , vol.17 , pp. 4848-4858
    • Bai, Y.1    Attardi, G.2
  • 36
    • 0032561134 scopus 로고    scopus 로고
    • Involvement of two novel chaperones in the assembly of mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Kuffner R., Rohr A., Schmiede A., Krull C., and Schulte U. Involvement of two novel chaperones in the assembly of mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Mol. Biol. 283 (1998) 409-417
    • (1998) J. Mol. Biol. , vol.283 , pp. 409-417
    • Kuffner, R.1    Rohr, A.2    Schmiede, A.3    Krull, C.4    Schulte, U.5
  • 38
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: A dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: A dawn for evolutionary medicine. Annu. Rev. Genet. 39 (2005) 359-407
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.