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Volumn 110, Issue 47, 2013, Pages 18934-18939

Assembly factors for the membrane arm of human complex i

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; MITOCHONDRIAL DNA; PROTEIN C3ORF1; PROTEIN NDUFA11; PROTEIN TMEM126B; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG;

EID: 84888110966     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1319247110     Document Type: Article
Times cited : (119)

References (47)
  • 1
    • 84874352529 scopus 로고    scopus 로고
    • Crystal structure of the entire respiratory complex i
    • Baradaran R, Berrisford JM, Minhas GS, Sazanov LA (2013) Crystal structure of the entire respiratory complex I. Nature 494(7438-443-448.
    • (2013) Nature , vol.494 , Issue.7438 , pp. 443-448
    • Baradaran, R.1    Berrisford, J.M.2    Minhas, G.S.3    Sazanov, L.A.4
  • 2
    • 0027104114 scopus 로고
    • The NADH: Ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker JE (1992) The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q Rev Biophys 25(3-253-324.
    • (1992) Q Rev Biophys , vol.25 , Issue.3 , pp. 253-324
    • Walker, J.E.1
  • 3
  • 4
    • 84865771586 scopus 로고    scopus 로고
    • NDUFA4 is a subunit of complex IV of the mammalian electron transport chain
    • Balsa E, et al. (2012) NDUFA4 is a subunit of complex IV of the mammalian electron transport chain. Cell Metab 16(3-378-386.
    • (2012) Cell Metab , vol.16 , Issue.3 , pp. 378-386
    • Balsa, E.1
  • 5
    • 0021866528 scopus 로고
    • Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase
    • Chomyn A, et al. (1985) Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature 314(6012- 592-597.
    • (1985) Nature , vol.314 , Issue.6012 , pp. 592-597
    • Chomyn, A.1
  • 7
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex i from Thermus thermophilus
    • Sazanov LA, Hinchliffe P (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311(5766-1430-1436.
    • (2006) Science , vol.311 , Issue.5766 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 9
    • 80052097536 scopus 로고    scopus 로고
    • Respiratory complex : Steam engine of the cell?
    • Efremov RG, Sazanov LA (2011) Respiratory complex I: 'Steam engine' of the cell? Curr Opin Struct Biol 21(4-532-540.
    • (2011) Curr Opin Struct Biol , vol.21 , Issue.4 , pp. 532-540
    • Efremov, R.G.1    Sazanov, L.A.2
  • 10
    • 0026472383 scopus 로고
    • Resolution of NADH: Ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme
    • Finel M, Skehel JM, Albracht SP, Fearnley IM, Walker JE (1992) Resolution of NADH: ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme. Biochemistry 31(46- 11425-11434.
    • (1992) Biochemistry , vol.31 , Issue.46 , pp. 11425-11434
    • Finel, M.1    Skehel, J.M.2    Albracht, S.P.3    Fearnley, I.M.4    Walker, J.E.5
  • 11
    • 0034691280 scopus 로고    scopus 로고
    • Resolution of the membrane domain of bovine complex i into subcomplexes: Implications for the structural organization of the enzyme
    • Sazanov LA, Peak-Chew SY, Fearnley IM, Walker JE (2000) Resolution of the membrane domain of bovine complex I into subcomplexes: Implications for the structural organization of the enzyme. Biochemistry 39(24-7229-7235.
    • (2000) Biochemistry , vol.39 , Issue.24 , pp. 7229-7235
    • Sazanov, L.A.1    Peak-Chew, S.Y.2    Fearnley, I.M.3    Walker, J.E.4
  • 12
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial complex i
    • Hunte C, Zickermann V, Brandt U (2010) Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science 329(5990-448-451.
    • (2010) Science , vol.329 , Issue.5990 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 13
    • 79959714122 scopus 로고    scopus 로고
    • A scaffold of accessory subunits links the peripheral arm and the distal proton-pumping module of mitochondrial complex i
    • Angerer H, et al. (2011) A scaffold of accessory subunits links the peripheral arm and the distal proton-pumping module of mitochondrial complex I. Biochem J 437(2- 279-288.
    • (2011) Biochem J , vol.437 , Issue.2 , pp. 279-288
    • Angerer, H.1
  • 14
    • 34250164233 scopus 로고    scopus 로고
    • Analysis of the assembly profiles for mitochondrial- and nuclear-DNA-encoded subunits into complex i
    • Lazarou M, McKenzie M, Ohtake A, Thorburn DR, Ryan MT (2007) Analysis of the assembly profiles for mitochondrial- and nuclear-DNA-encoded subunits into complex I. Mol Cell Biol 27(12-4228-4237.
    • (2007) Mol Cell Biol , vol.27 , Issue.12 , pp. 4228-4237
    • Lazarou, M.1    McKenzie, M.2    Ohtake, A.3    Thorburn, D.R.4    Ryan, M.T.5
  • 15
    • 77955872123 scopus 로고    scopus 로고
    • Assembly factors of human mitochondrial complex i and their defects in disease
    • McKenzieM, Ryan MT (2010) Assembly factors of human mitochondrial complex I and their defects in disease. IUBMB Life 62(7-497-502.
    • (2010) IUBMB Life , vol.62 , Issue.7 , pp. 497-502
    • McKenziem Ryan, M.T.1
  • 17
    • 41849090449 scopus 로고    scopus 로고
    • Mitochondrial complex i deficiency caused by a deleterious NDUFA11 mutation
    • Berger I, et al. (2008) Mitochondrial complex I deficiency caused by a deleterious NDUFA11 mutation. Ann Neurol 63(3-405-408.
    • (2008) Ann Neurol , vol.63 , Issue.3 , pp. 405-408
    • Berger, I.1
  • 18
    • 84863012272 scopus 로고    scopus 로고
    • Molecular diagnosis of infantile mitochondrial disease with targeted next-generation sequencing
    • Calvo SE, et al. (2012) Molecular diagnosis of infantile mitochondrial disease with targeted next-generation sequencing. Sci Transl Med 4(118-118ra10.
    • (2012) Sci Transl Med , vol.4 , Issue.118
    • Calvo, S.E.1
  • 19
    • 33846846449 scopus 로고    scopus 로고
    • X-linked NDUFA1 gene mutations associated with mitochondrial encephalomyopathy
    • Fernandez-Moreira D, et al. (2007) X-linked NDUFA1 gene mutations associated with mitochondrial encephalomyopathy. Ann Neurol 61(1-73-83.
    • (2007) Ann Neurol , vol.61 , Issue.1 , pp. 73-83
    • Fernandez-Moreira, D.1
  • 20
    • 84855987219 scopus 로고    scopus 로고
    • Mutation screening of 75 candidate genes in 152 complex i deficiency cases identifies pathogenic variants in 16 genes including NDUFB9
    • Haack TB, et al. (2012) Mutation screening of 75 candidate genes in 152 complex I deficiency cases identifies pathogenic variants in 16 genes including NDUFB9. J Med Genet 49(2-83-89.
    • (2012) J Med Genet , vol.49 , Issue.2 , pp. 83-89
    • Haack, T.B.1
  • 21
    • 44449163314 scopus 로고    scopus 로고
    • NDUFA2 complex i mutation leads to Leigh disease
    • Hoefs SJ, et al. (2008) NDUFA2 complex I mutation leads to Leigh disease. Am J Hum Genet 82(6-1306-1315.
    • (2008) Am J Hum Genet , vol.82 , Issue.6 , pp. 1306-1315
    • Hoefs, S.J.1
  • 22
    • 79951811473 scopus 로고    scopus 로고
    • NDUFA10 mutations cause complex i deficiency in a patient with Leigh disease
    • Hoefs SJ, et al. (2011) NDUFA10 mutations cause complex I deficiency in a patient with Leigh disease. Eur J Hum Genet 19(3-270-274.
    • (2011) Eur J Hum Genet , vol.19 , Issue.3 , pp. 270-274
    • Hoefs, S.J.1
  • 23
    • 8844244960 scopus 로고    scopus 로고
    • NDUFS6 mutations are a novel cause of lethal neonatal mitochondrial complex i deficiency
    • Kirby DM, et al. (2004) NDUFS6 mutations are a novel cause of lethal neonatal mitochondrial complex I deficiency. J Clin Invest 114(6-837-845.
    • (2004) J Clin Invest , vol.114 , Issue.6 , pp. 837-845
    • Kirby, D.M.1
  • 24
    • 81055158015 scopus 로고    scopus 로고
    • Respiratory chain complex i deficiency due to NDUFA12 mutations as a new cause of Leigh syndrome
    • Ostergaard E, et al. (2011) Respiratory chain complex I deficiency due to NDUFA12 mutations as a new cause of Leigh syndrome. J Med Genet 48(11-737-740.
    • (2011) J Med Genet , vol.48 , Issue.11 , pp. 737-740
    • Ostergaard, E.1
  • 25
    • 84856008577 scopus 로고    scopus 로고
    • Defective NDUFA9 as a novel cause of neonatally fatal complex i disease
    • van den Bosch BJ, et al. (2012) Defective NDUFA9 as a novel cause of neonatally fatal complex I disease. J Med Genet 49(1-10-15.
    • (2012) J Med Genet , vol.49 , Issue.1 , pp. 10-15
    • Van Den Bosch, B.J.1
  • 26
    • 17344365132 scopus 로고    scopus 로고
    • Demonstration of a new pathogenic mutation in human complex i deficiency: A 5-bp duplication in the nuclear gene encoding the 18- kD (AQDQ) subunit
    • van den Heuvel L, et al. (1998) Demonstration of a new pathogenic mutation in human complex I deficiency: A 5-bp duplication in the nuclear gene encoding the 18- kD (AQDQ) subunit. Am J Hum Genet 62(2-262-268.
    • (1998) Am J Hum Genet , vol.62 , Issue.2 , pp. 262-268
    • Van Den Heuvel, L.1
  • 27
    • 84867101923 scopus 로고    scopus 로고
    • Complexome profiling identifies TMEM126B as a component of the mitochondrial complex i assembly complex
    • Heide H, et al. (2012) Complexome profiling identifies TMEM126B as a component of the mitochondrial complex I assembly complex. Cell Metab 16(4-538-549.
    • (2012) Cell Metab , vol.16 , Issue.4 , pp. 538-549
    • Heide, H.1
  • 28
    • 34248576290 scopus 로고    scopus 로고
    • Investigation of the complex i assembly chaperones B17.2L and NDUFAF1 in a cohort of CI deficient patients
    • Vogel RO, et al. (2007) Investigation of the complex I assembly chaperones B17.2L and NDUFAF1 in a cohort of CI deficient patients. Mol Genet Metab 91(2-176-182.
    • (2007) Mol Genet Metab , vol.91 , Issue.2 , pp. 176-182
    • Vogel, R.O.1
  • 29
    • 78649454768 scopus 로고    scopus 로고
    • FOXRED1, encoding an FAD-dependent oxidoreductase complex-I-specific molecular chaperone, is mutated in infantile-onset mitochondrial encephalopathy
    • Fassone E, et al. (2010) FOXRED1, encoding an FAD-dependent oxidoreductase complex-I-specific molecular chaperone, is mutated in infantile-onset mitochondrial encephalopathy. Hum Mol Genet 19(24-4837-4847.
    • (2010) Hum Mol Genet , vol.19 , Issue.24 , pp. 4837-4847
    • Fassone, E.1
  • 30
    • 66749128531 scopus 로고    scopus 로고
    • Mutations in NDUFAF3 (C3ORF60), encoding an NDUFAF4 (C6ORF66)-interacting complex i assembly protein, cause fatal neonatal mitochondrial disease
    • Saada A, et al. (2009) Mutations in NDUFAF3 (C3ORF60), encoding an NDUFAF4 (C6ORF66)-interacting complex I assembly protein, cause fatal neonatal mitochondrial disease. Am J Hum Genet 84(6-718-727.
    • (2009) Am J Hum Genet , vol.84 , Issue.6 , pp. 718-727
    • Saada, A.1
  • 31
    • 77956318447 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex i
    • Nouws J, et al. (2010) Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex I. Cell Metab 12(3-283-294.
    • (2010) Cell Metab , vol.12 , Issue.3 , pp. 283-294
    • Nouws, J.1
  • 32
    • 33947129099 scopus 로고    scopus 로고
    • Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex i assembly
    • Vogel RO, et al. (2007) Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex I assembly. Genes Dev 21(5-615-624.
    • (2007) Genes Dev , vol.21 , Issue.5 , pp. 615-624
    • Vogel, R.O.1
  • 33
    • 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, et al. (2004) Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: A framework to interpret complex I deficiencies. Hum Mol Genet 13(20-2461-2472.
    • (2004) Hum Mol Genet , vol.13 , Issue.20 , pp. 2461-2472
    • Ugalde, C.1
  • 34
    • 66449128208 scopus 로고    scopus 로고
    • Down-regulation of mitochondrial acyl carrier protein in mammalian cells compromises protein lipoylation and respiratory complex i and results in cell death
    • Feng D, Witkowski A, Smith S (2009) Down-regulation of mitochondrial acyl carrier protein in mammalian cells compromises protein lipoylation and respiratory complex I and results in cell death. J Biol Chem 284(17-11436-11445.
    • (2009) J Biol Chem , vol.284 , Issue.17 , pp. 11436-11445
    • Feng, D.1    Witkowski, A.2    Smith, S.3
  • 35
    • 0026484793 scopus 로고
    • Conservation of sequences of subunits of mitochondrial complex i and their relationships with other proteins
    • Fearnley IM, Walker JE (1992) Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins. Biochim Biophys Acta 1140(2- 105-134.
    • (1992) Biochim Biophys Acta , vol.1140 , Issue.2 , pp. 105-134
    • Fearnley, I.M.1    Walker, J.E.2
  • 36
    • 0042925385 scopus 로고    scopus 로고
    • The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3
    • Zhang J, et al. (2003) The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3. Proc Natl Acad Sci USA 100(16-9342-9347.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.16 , pp. 9342-9347
    • Zhang, J.1
  • 37
    • 4444353420 scopus 로고    scopus 로고
    • The oxidized subunit B8 from human complex i adopts a thioredoxin fold
    • Brockmann C, et al. (2004) The oxidized subunit B8 from human complex I adopts a thioredoxin fold. Structure 12(9-1645-1654.
    • (2004) Structure , vol.12 , Issue.9 , pp. 1645-1654
    • Brockmann, C.1
  • 38
    • 26444488636 scopus 로고    scopus 로고
    • A molecular chaperone for mitochondrial complex i assembly is mutated in a progressive encephalopathy
    • Ogilvie I, Kennaway NG, Shoubridge EA (2005) A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy. J Clin Invest 115(10-2784-2792.
    • (2005) J Clin Invest , vol.115 , Issue.10 , pp. 2784-2792
    • Ogilvie, I.1    Kennaway, N.G.2    Shoubridge, E.A.3
  • 40
    • 53049098744 scopus 로고    scopus 로고
    • Mutation of C20orf7 disrupts complex i assembly and causes lethal neonatal mitochondrial disease
    • Sugiana C, et al. (2008) Mutation of C20orf7 disrupts complex I assembly and causes lethal neonatal mitochondrial disease. Am J Hum Genet 83(4-468-478.
    • (2008) Am J Hum Genet , vol.83 , Issue.4 , pp. 468-478
    • Sugiana, C.1
  • 41
    • 82555168324 scopus 로고    scopus 로고
    • Mutations in the gene encoding C8orf38 block complex i assembly by inhibiting production of the mitochondria-encoded subunit ND1
    • McKenzie M, et al. (2011) Mutations in the gene encoding C8orf38 block complex I assembly by inhibiting production of the mitochondria-encoded subunit ND1. J Mol Biol 414(3-413-426.
    • (2011) J Mol Biol , vol.414 , Issue.3 , pp. 413-426
    • McKenzie, M.1
  • 42
    • 71949116823 scopus 로고    scopus 로고
    • Human ind1, an iron-sulfur cluster assembly factor for respiratory complex i
    • Sheftel AD, et al. (2009) Human ind1, an iron-sulfur cluster assembly factor for respiratory complex I. Mol Cell Biol 29(22-6059-6073.
    • (2009) Mol Cell Biol , vol.29 , Issue.22 , pp. 6059-6073
    • Sheftel, A.D.1
  • 43
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • Chacinska A, Koehler CM, Milenkovic D, Lithgow T, Pfanner N (2009) Importing mitochondrial proteins: machineries and mechanisms. Cell 138(4-628-644.
    • (2009) Cell , vol.138 , Issue.4 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 44
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, et al. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1(5- 376-386.
    • (2002) Mol Cell Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1
  • 45
    • 79953701087 scopus 로고    scopus 로고
    • Andromeda: A peptide search engine integrated into the Max- Quant environment
    • Cox J, et al. (2011) Andromeda: A peptide search engine integrated into the Max- Quant environment. J Proteome Res 10(4-1794-1805.
    • (2011) J Proteome Res , vol.10 , Issue.4 , pp. 1794-1805
    • Cox, J.1
  • 46
    • 79959424627 scopus 로고    scopus 로고
    • Quantitative, high-resolution proteomics for data-driven systems biology
    • Cox J, Mann M (2011) Quantitative, high-resolution proteomics for data-driven systems biology. Annu Rev Biochem 80:273-299.
    • (2011) Annu Rev Biochem , vol.80 , pp. 273-299
    • Cox, J.1    Mann, M.2
  • 47
    • 72449176842 scopus 로고    scopus 로고
    • The structure of eukaryotic and prokaryotic complex i
    • Clason T, et al. (2010) The structure of eukaryotic and prokaryotic complex I. J Struct Biol 169(1-81-88.
    • (2010) J Struct Biol , vol.169 , Issue.1 , pp. 81-88
    • Clason, T.1


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