메뉴 건너뛰기




Volumn 13, Issue 6, 2004, Pages 659-667

Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; PROTEIN SUBUNIT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 1642382090     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/ddh071     Document Type: Article
Times cited : (185)

References (48)
  • 1
    • 0035349906 scopus 로고    scopus 로고
    • The genetics and pathology of oxidative phosphorylation
    • Smeitink, J., van den Heuvel, L. and DiMauro, S. (2001) The genetics and pathology of oxidative phosphorylation. Nat. Rev. Genet., 2, 342-352.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 342-352
    • Smeitink, J.1    van den Heuvel, L.2    DiMauro, S.3
  • 9
    • 0035283150 scopus 로고    scopus 로고
    • A nonsense mutation in the NDUFS4 gene encoding the 18 kDa (AQDQ) subunit of complex I abolishes assembly and activity of the complex in a patient with Leigh-like syndrome
    • Petruzzella, V., Vergari, R., Puzziferri, I., Boffoli, D., Lamantea, E., Zeviani, M. and Papa, S. (2001) A nonsense mutation in the NDUFS4 gene encoding the 18 kDa (AQDQ) subunit of complex I abolishes assembly and activity of the complex in a patient with Leigh-like syndrome. Hum. Mol. Genet., 10, 529-535.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 529-535
    • Petruzzella, V.1    Vergari, R.2    Puzziferri, I.3    Boffoli, D.4    Lamantea, E.5    Zeviani, M.6    Papa, S.7
  • 10
    • 0037943964 scopus 로고    scopus 로고
    • Genotyping microsatellite DNA markers at putative disease loci in inbred/multiplex families with respiratory chain complex I deficiency allows rapid identification of a novel nonsense mutation (IVS1nt-1) in the NDUFS4 gene in Leigh syndrome
    • Benit, P., Steffann, J., Lebon, S., Chretien, D., Kadhom, N., de Lonlay, P., Goldenberg, A., Dumez, Y., Dommergues, M., Rustin, P. et al. (2003) Genotyping microsatellite DNA markers at putative disease loci in inbred/multiplex families with respiratory chain complex I deficiency allows rapid identification of a novel nonsense mutation (IVS1nt-1) in the NDUFS4 gene in Leigh syndrome. Hum. Genet., 112, 563-566.
    • (2003) Hum. Genet. , vol.112 , pp. 563-566
    • Benit, P.1    Steffann, J.2    Lebon, S.3    Chretien, D.4    Kadhom, N.5    de Lonlay, P.6    Goldenberg, A.7    Dumez, Y.8    Dommergues, M.9    Rustin, P.10
  • 14
    • 0036803084 scopus 로고    scopus 로고
    • The energy-transducing NADH: Quinone oxidoreductase, complex I
    • Yano, T. (2002) The energy-transducing NADH: Quinone oxidoreductase, complex I. Mol. Asp. Med., 23, 345-368.
    • (2002) Mol. Asp. Med. , vol.23 , pp. 345-368
    • Yano, T.1
  • 15
    • 0034663704 scopus 로고    scopus 로고
    • Application of the obligate aerobic yeast Yarrowia lipolytica as a eucaryotic model to analyse Leigh syndrome mutations in the complex I core subunits PSST and TYKY
    • Ahlers, P.M., Garofano, A., Kerscher, S.J. and Brandt, U. (2000) Application of the obligate aerobic yeast Yarrowia lipolytica as a eucaryotic model to analyse Leigh syndrome mutations in the complex I core subunits PSST and TYKY. Biochim. Biophys. Acta, 1459, 258-265.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 258-265
    • Ahlers, P.M.1    Garofano, A.2    Kerscher, S.J.3    Brandt, U.4
  • 17
    • 0035793474 scopus 로고    scopus 로고
    • Mutation in the NDUFS4 gene of complex I abolishes cAMP-dependent activation of the complex in a child with fatal neurological syndrome
    • Papa, S., Scacco, S., Sardanelli, A.M., Vergari, R., Papa, F., Budde, S., van den Heuvel, L. and Smeitink, J. (2001) Mutation in the NDUFS4 gene of complex I abolishes cAMP-dependent activation of the complex in a child with fatal neurological syndrome. FEBS Lett., 489, 259-262.
    • (2001) FEBS Lett. , vol.489 , pp. 259-262
    • Papa, S.1    Scacco, S.2    Sardanelli, A.M.3    Vergari, R.4    Papa, F.5    Budde, S.6    van den Heuvel, L.7    Smeitink, J.8
  • 18
    • 0242414752 scopus 로고    scopus 로고
    • Pathological mutations of the human NDUFS4 gene of the 18-kDa (AQDQ) subunit of complex I affect the expression of the protein and the assembly and function of the complex
    • Scacco, S., Petruzzella, V., Budde, S., Vergari, R., Tamborra, R., Panelli, D., van den Heuvel, L.P., Smeitink, J.A. and Papa, S. (2003) Pathological mutations of the human NDUFS4 gene of the 18-kDa (AQDQ) subunit of complex I affect the expression of the protein and the assembly and function of the complex. J. Biol. Chem., 278, 44161-44167.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44161-44167
    • Scacco, S.1    Petruzzella, V.2    Budde, S.3    Vergari, R.4    Tamborra, R.5    Panelli, D.6    van den Heuvel, L.P.7    Smeitink, J.A.8    Papa, S.9
  • 20
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H. and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem., 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 22
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schagger, H. and Pfeiffer, K. (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
  • 23
    • 0033767317 scopus 로고    scopus 로고
    • An out-of-frame cytochrome b gene deletion from a patient with parkinsonism is associated with impaired complex III assembly and an increase in free radical production
    • Rana, M., de Coo, I., Diaz, F., Smeets, H. and Moraes, C.T. (2000) An out-of-frame cytochrome b gene deletion from a patient with parkinsonism is associated with impaired complex III assembly and an increase in free radical production. Ann. Neurol., 48, 774-781.
    • (2000) Ann. Neurol. , vol.48 , pp. 774-781
    • Rana, M.1    de Coo, I.2    Diaz, F.3    Smeets, H.4    Moraes, C.T.5
  • 26
    • 0037314215 scopus 로고    scopus 로고
    • Neuronal degeneration and mitochondrial dysfunction
    • Schon, E.A. and Manfredi, G. (2003) Neuronal degeneration and mitochondrial dysfunction. J. Clin. Invest., 111, 303-312.
    • (2003) J. Clin. Invest. , vol.111 , pp. 303-312
    • Schon, E.A.1    Manfredi, G.2
  • 28
    • 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. (2002) Species-specific and mutant MWFE proteins. Their effect on the assembly of a functional mammalian mitochondrial complex I. J. Biol. Chem., 277, 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
  • 29
    • 0037056054 scopus 로고    scopus 로고
    • From NADH to ubiquinone in Neurospora mitochondria
    • Videira, A. and Duarte, M. (2002) From NADH to ubiquinone in Neurospora mitochondria. Biochim. Biophys. Acta, 1555, 187-191.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 187-191
    • Videira, A.1    Duarte, M.2
  • 30
    • 0034604568 scopus 로고    scopus 로고
    • Function of conserved acidic residues in the PSST homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica
    • Ahlers, P.M., Zwicker, K., Kerscher, S. and Brandt, U. (2000) Function of conserved acidic residues in the PSST homologue of complex I (NADH:uBiquinone oxidoreductase) from Yarrowia lipolytica. J. Biol. Chem., 275, 23577-23582.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23577-23582
    • Ahlers, P.M.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 31
    • 0035968167 scopus 로고    scopus 로고
    • A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I
    • Kashani-Poor, N., Zwicker, K., Kerscher, S. and Brandt, U. (2001) A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I. J. Biol. Chem., 276, 24082-24087.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24082-24087
    • Kashani-Poor, N.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 32
    • 0028848235 scopus 로고
    • Generation and characterization of NADH: Ubiquinone oxidoreductase mutants in Neurospora crassa
    • Schulte, U. and Weiss, H. (1995) Generation and characterization of NADH: Ubiquinone oxidoreductase mutants in Neurospora crassa. Meth. Enzymol., 260, 3-14.
    • (1995) Meth. Enzymol. , vol.260 , pp. 3-14
    • Schulte, U.1    Weiss, H.2
  • 33
    • 0033785845 scopus 로고    scopus 로고
    • Respiratory chain complex I is essential for sexual development in Neurospora and binding of iron sulfur clusters are required for enzyme assembly
    • Duarte, M. and Videira, A. (2000) Respiratory chain complex I is essential for sexual development in Neurospora and binding of iron sulfur clusters are required for enzyme assembly. Genetics, 156, 607-615.
    • (2000) Genetics , vol.156 , pp. 607-615
    • Duarte, M.1    Videira, A.2
  • 34
    • 0037096980 scopus 로고    scopus 로고
    • Disruption of iron-sulphur cluster N2 from NADH: Ubiquinone oxidoreductase by site-directed mutagenesis
    • Duarte, M., Populo, H., Videira, A., Friedrich, T. and Schulte, U. (2002) Disruption of iron-sulphur cluster N2 from NADH: ubiquinone oxidoreductase by site-directed mutagenesis. Biochem. J., 364, 833-839.
    • (2002) Biochem. J. , vol.364 , pp. 833-839
    • Duarte, M.1    Populo, H.2    Videira, A.3    Friedrich, T.4    Schulte, U.5
  • 35
    • 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. (2003) Identification and characterization of a common set of complex I assembly intermediates in mitochondria from patients with complex I deficiency. J. Biol. Chem., 278, 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
  • 36
    • 0036523991 scopus 로고    scopus 로고
    • CIA30 complex I assembly factor: A candidate for human complex I deficiency?
    • Janssen, R., Smeitink, J., Smeets, R. and van den Heuvel, L. (2002) CIA30 complex I assembly factor: A candidate for human complex I deficiency? Hum. Genet., 110, 264-270.
    • (2002) Hum. Genet. , vol.110 , pp. 264-270
    • Janssen, R.1    Smeitink, J.2    Smeets, R.3    van den Heuvel, L.4
  • 37
    • 0037056042 scopus 로고    scopus 로고
    • The NDUFS4 nuclear gene of complex I of mitochondria and the cAMP cascade
    • Papa, S. (2002) The NDUFS4 nuclear gene of complex I of mitochondria and the cAMP cascade. Biochim. Biophys. Acta, 1555, 147-153.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 147-153
    • Papa, S.1
  • 38
    • 0038034950 scopus 로고    scopus 로고
    • Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye
    • Schulenberg, B., Aggeler, R., Beechem, J.M., Capaldi, R.A. and Patton, W.F. (2003) Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J. Biol. Chem., 278, 27251-27255.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27251-27255
    • Schulenberg, B.1    Aggeler, R.2    Beechem, J.M.3    Capaldi, R.A.4    Patton, W.F.5
  • 39
    • 0035937792 scopus 로고    scopus 로고
    • Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria. evidence for the slow active/inactive transition
    • Grivennikova, V.G., Kapustin, A.N. and Vinogradov, A.D. (2001) Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria. evidence for the slow active/inactive transition. J. Biol. Chem., 276, 9038-9044.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9038-9044
    • Grivennikova, V.G.1    Kapustin, A.N.2    Vinogradov, A.D.3
  • 40
    • 0037124043 scopus 로고    scopus 로고
    • A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    • Bottcher, B., Scheide, D., Hesterberg, M., Nagel-Steger, L. and Friedrich, T. (2002) A novel, enzymatically active conformation of the Escherichia coli NADH:uBiquinone oxidoreductase (complex I). J. Biol. Chem., 277, 17970-17977.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17970-17977
    • Bottcher, B.1    Scheide, D.2    Hesterberg, M.3    Nagel-Steger, L.4    Friedrich, T.5
  • 41
    • 0037325411 scopus 로고    scopus 로고
    • The transition between active and de-activated forms of NADH: Ubiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa
    • Grivennikova, V.G., Serebryanaya, D.V., Isakova, E.P., Belozerskaya, T.A. and Vinogradov, A.D. (2003) The transition between active and de-activated forms of NADH:uBiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa. Biochem. J., 369, 619-626.
    • (2003) Biochem. J. , vol.369 , pp. 619-626
    • Grivennikova, V.G.1    Serebryanaya, D.V.2    Isakova, E.P.3    Belozerskaya, T.A.4    Vinogradov, A.D.5
  • 42
    • 0036132671 scopus 로고    scopus 로고
    • A novel nonsense mutation (Q352X) in the mitochondrial cytochrome b gene associated with a combined deficiency of complexes I and III
    • Lamantea, E., Carrara, F., Mariotti, C., Morandi, L., Tiranti, V. and Zeviani, M. (2002) A novel nonsense mutation (Q352X) in the mitochondrial cytochrome b gene associated with a combined deficiency of complexes I and III. Neuromusc. Disord., 12, 49-52.
    • (2002) Neuromusc. Disord. , vol.12 , pp. 49-52
    • Lamantea, E.1    Carrara, F.2    Mariotti, C.3    Morandi, L.4    Tiranti, V.5    Zeviani, M.6
  • 43
    • 0037056045 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes of mitochondria and bacteria
    • Sebagger, H. (2002) Respiratory chain supercomplexes of mitochondria and bacteria. Biochim. Biophys. Acta, 1555, 154-159.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 154-159
    • Sebagger, H.1
  • 44
    • 0043208847 scopus 로고    scopus 로고
    • Functional implications from an unexpected position of the 49-kDa subunit of NADH: Ubiquinone oxidoreductase
    • Zickermann, V., Bostina, M., Hunte, C., Ruiz, T., Radermacher, M. and Brandt, U. (2003) Functional implications from an unexpected position of the 49-kDa subunit of NADH:uBiquinone oxidoreductase. J. Biol. Chem., 278, 29072-29078.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29072-29078
    • Zickermann, V.1    Bostina, M.2    Hunte, C.3    Ruiz, T.4    Radermacher, M.5    Brandt, U.6
  • 45
    • 0027408368 scopus 로고
    • Mitochondrial NADH:ubiquinone oxidoreductase (complex I): Proximity of the subunits of the flavoprotein and the iron-sulfur protein subcomplexes
    • Yamaguchi, M. and Hatefi, Y. (1993) Mitochondrial NADH:uBiquinone oxidoreductase (Pomplex I): proximity of the subunits of the flavoprotein and the iron-sulfur protein subcomplexes. Biochemistry, 32, 1935-1939.
    • (1993) Biochemistry , vol.32 , pp. 1935-1939
    • Yamaguchi, M.1    Hatefi, Y.2
  • 46
    • 1042268861 scopus 로고    scopus 로고
    • Mitochondrial complex I mutations in Caenorhabditis elegans produce cytochrome c oxidase deficiency, oxidative stress, and vitamin-responsive lactic acidosis
    • Grad, L.I. and Lemire B.D. (2004) Mitochondrial complex I mutations in Caenorhabditis elegans produce cytochrome c oxidase deficiency, oxidative stress, and vitamin-responsive lactic acidosis. Hum. Mol. Genet., 13, 303-314.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 303-314
    • Grad, L.I.1    Lemire, B.D.2
  • 47
    • 0030015691 scopus 로고    scopus 로고
    • Lethal infantile mitochondrial disease with isolated complex I deficiency in fibroblasts but with combined complex I and IV deficiencies in muscle
    • Bentlage, H.A., Wendel, U., Schagger, H., ter Laak, H.J., Janssen, A.J. and Trijbels, J.M. (1996) Lethal infantile mitochondrial disease with isolated complex I deficiency in fibroblasts but with combined complex I and IV deficiencies in muscle. Neurology, 47, 243-248.
    • (1996) Neurology , vol.47 , pp. 243-248
    • Bentlage, H.A.1    Wendel, U.2    Schagger, H.3    ter Laak, H.J.4    Janssen, A.J.5    Trijbels, J.M.6
  • 48
    • 0036024975 scopus 로고    scopus 로고
    • Blue Native electrophoresis to study mitochondrial and other protein complexes
    • Nijtmans, L.G., Henderson, N.S. and Holt, I.J. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.