메뉴 건너뛰기




Volumn 1659, Issue 2-3, 2004, Pages 197-205

Application of the yeast Yarrowia lipolytica as a model to analyse human pathogenic mutations in mitochondrial complex I (NADH:ubiquinone oxidoreductase)

Author keywords

Complex I; Mutation; Yarrowia lipolytica

Indexed keywords

CYTOCHROME C OXIDASE; ENZYME INHIBITOR; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UBIQUINONE;

EID: 9644283053     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.07.006     Document Type: Conference Paper
Times cited : (32)

References (51)
  • 1
    • 0035968167 scopus 로고    scopus 로고
    • A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I
    • N. Kashani-Poor, K. Zwicker, S. Kerscher, and U. Brandt A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I J. Biol. Chem. 276 2001 24082 24087
    • (2001) J. Biol. Chem. , vol.276 , pp. 24082-24087
    • Kashani-Poor, N.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 3
    • 0034691658 scopus 로고    scopus 로고
    • Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica
    • R. Djafarzadeh, S. Kerscher, K. Zwicker, M. Radermacher, M. Lindahl, H. Schägger, and U. Brandt Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica Biochim. Biophys. Acta 1459 2000 230 238
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 230-238
    • Djafarzadeh, R.1    Kerscher, S.2    Zwicker, K.3    Radermacher, M.4    Lindahl, M.5    Schägger, H.6    Brandt, U.7
  • 4
    • 0026077298 scopus 로고
    • Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I)
    • G. Hofhaus, H. Weiss, and K. Leonard Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I) J. Mol. Biol. 221 1991 1027 1043
    • (1991) J. Mol. Biol. , vol.221 , pp. 1027-1043
    • Hofhaus, G.1    Weiss, H.2    Leonard, K.3
  • 5
    • 0032512616 scopus 로고    scopus 로고
    • Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • V. Guenebaut, A. Schlitt, H. Weiss, K. Leonard, and T. Friedrich Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I) J. Mol. Biol. 276 1998 105 112
    • (1998) J. Mol. Biol. , vol.276 , pp. 105-112
    • Guenebaut, V.1    Schlitt, A.2    Weiss, H.3    Leonard, K.4    Friedrich, T.5
  • 6
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (Complex I) at 22 Å in ice
    • N. Grigorieff Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (Complex I) at 22 Å in ice J. Mol. Biol. 277 1998 1033 1046
    • (1998) J. Mol. Biol. , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 9
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters semiquinones in Complex I
    • T. Ohnishi Iron-sulfur clusters semiquinones in Complex I Biochim. Biophys. Acta 1364 1998 186 206
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 10
    • 0021769852 scopus 로고
    • Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone
    • M.K.F. Wikström Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone FEBS Lett. 169 1984 300 304
    • (1984) FEBS Lett. , vol.169 , pp. 300-304
    • Wikström, M.K.F.1
  • 11
    • 0035297567 scopus 로고    scopus 로고
    • - stoichiometry of the NADH: Ubiquinone reductase reaction catalyzed by submitochondrial particles
    • - stoichiometry of the NADH: ubiquinone reductase reaction catalyzed by submitochondrial particles Biochemistry (Moscow) 66 2001 435 443
    • (2001) Biochemistry (Moscow) , vol.66 , pp. 435-443
    • Galkin, A.S.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 12
    • 2442685843 scopus 로고    scopus 로고
    • The role of oxidative damage in mitochondria during aging: A review
    • H. Huang, and G. Manton The role of oxidative damage in mitochondria during aging: a review Front. Biosci. 9 2004 1100 1117
    • (2004) Front. Biosci. , vol.9 , pp. 1100-1117
    • Huang, H.1    Manton, G.2
  • 18
    • 0032490099 scopus 로고    scopus 로고
    • Human Complex I deficiency: Clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect
    • B.H. Robinson Human Complex I deficiency: Clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect Biochim. Biophys. Acta 1364 1998 271 286
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 271-286
    • Robinson, B.H.1
  • 20
    • 3543043510 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification
    • I. Rais, M. Karas, and H. Schägger Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification Proteomics 2004 (in press)
    • (2004) Proteomics
    • Rais, I.1    Karas, M.2    Schägger, H.3
  • 22
    • 0034663640 scopus 로고    scopus 로고
    • Diversity and origin of alternative NADH:ubiquinone oxidoreductases
    • S. Kerscher Diversity and origin of alternative NADH:ubiquinone oxidoreductases. Biochim. Biophys. Acta 1459 2000 274 283
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 274-283
    • Kerscher, S.1
  • 23
    • 0032812743 scopus 로고    scopus 로고
    • T. A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica
    • S. Kerscher, J.G. Okun, and U. Br t. A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica J. Cell Sci. 112 1999 2347 2354
    • (1999) J. Cell Sci. , vol.112 , pp. 2347-2354
    • Kerscher, S.1    Okun, J.G.2    Br, U.3
  • 24
    • 0035179011 scopus 로고    scopus 로고
    • External alternative NADH:ubiquinone oxidoreductase redirected to the internal face of the mitochondrial inner membrane rescues complex I deficiency in Yarrowia lipolytica
    • S. Kerscher, A. Eschemann, P.M. Okun, and U. Brandt External alternative NADH:ubiquinone oxidoreductase redirected to the internal face of the mitochondrial inner membrane rescues complex I deficiency in Yarrowia lipolytica J. Cell Sci. 114 2001 3915 3921
    • (2001) J. Cell Sci. , vol.114 , pp. 3915-3921
    • Kerscher, S.1    Eschemann, A.2    Okun, P.M.3    Brandt, U.4
  • 25
    • 0035795187 scopus 로고    scopus 로고
    • Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica
    • N. Kashani-Poor, S. Kerscher, V. Zickermann, and U. Brandt Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica Biochim. Biophys. Acta 1504 2001 363 370
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 363-370
    • Kashani-Poor, N.1    Kerscher, S.2    Zickermann, V.3    Brandt, U.4
  • 26
    • 0038392255 scopus 로고    scopus 로고
    • Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism?
    • U. Brandt, S. Kerscher, S. Dröse, K. Zwicker, and V. Zickermann Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism? FEBS Lett. 545 2003 9 17
    • (2003) FEBS Lett. , vol.545 , pp. 9-17
    • Brandt, U.1    Kerscher, S.2    Dröse, S.3    Zwicker, K.4    Zickermann, V.5
  • 27
    • 0034604568 scopus 로고    scopus 로고
    • Function of conserved acidic residues in the PSST-homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica
    • P. Ahlers, K. Zwicker, S. Kerscher, and U. Brand Function of conserved acidic residues in the PSST-homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica J. Biol. Chem. 275 2000 23577 23582
    • (2000) J. Biol. Chem. , vol.275 , pp. 23577-23582
    • Ahlers, P.1    Zwicker, K.2    Kerscher, S.3    Brand, U.4
  • 28
    • 0142149098 scopus 로고    scopus 로고
    • Two aspartic acid residues in the PSST-homologous NUKM subunit of complex I from Yarrowia lipolytica are essential for catalytic activity
    • A. Garofano, K. Zwicker, S. Kerscher, P. Okun, and U. Brandt Two aspartic acid residues in the PSST-homologous NUKM subunit of complex I from Yarrowia lipolytica are essential for catalytic activity J. Biol. Chem. 278 2003 42435 42440
    • (2003) J. Biol. Chem. , vol.278 , pp. 42435-42440
    • Garofano, A.1    Zwicker, K.2    Kerscher, S.3    Okun, P.4    Brandt, U.5
  • 29
    • 0037096980 scopus 로고    scopus 로고
    • Disruption of iron-sulphur cluster N2 from NADH:ubiquinone oxidoreductase by site-directed mutagenesis
    • M. Duarte, H. Populo, A. Videira, T. Friedrich, and U. Schulte Disruption of iron-sulphur cluster N2 from NADH:ubiquinone oxidoreductase by site-directed mutagenesis Biochem. J. 364 2002 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
  • 30
    • 0347481386 scopus 로고    scopus 로고
    • Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB
    • D. Flemming, A. Schlitt, V. Spehr, T. Bischof, and T. Friedrich Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB J. Biol. Chem. 278 2003 47602 47609
    • (2003) J. Biol. Chem. , vol.278 , pp. 47602-47609
    • Flemming, D.1    Schlitt, A.2    Spehr, V.3    Bischof, T.4    Friedrich, T.5
  • 31
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • R. Böhm, M. Sauter, and A. Böck Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components Mol. Microbiol. 4 1990 231 243
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 32
    • 0027328631 scopus 로고
    • Initimate relationships of the large and the small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH:ubiquinone oxidoreductase
    • S.P.J. Albracht Initimate relationships of the large and the small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH:ubiquinone oxidoreductase Biochim. Biophys. Acta 1144 1993 221 224
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 221-224
    • Albracht, S.P.J.1
  • 33
    • 0036523377 scopus 로고    scopus 로고
    • Hydrogenases: Hydrogen-activating enzymes
    • M. Frey Hydrogenases: hydrogen-activating enzymes ChemBioChem 3 2002 153 160
    • (2002) ChemBioChem , vol.3 , pp. 153-160
    • Frey, M.1
  • 34
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • T. Friedrich, and D. Scheide The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases FEBS Lett. 479 2000 1 5
    • (2000) FEBS Lett. , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 36
    • 0032504107 scopus 로고    scopus 로고
    • The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors
    • E. Darrouzet, J.P. Issartel, J. Lunardi, and A. Dupuis The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors FEBS Lett. 431 1998 34 38
    • (1998) FEBS Lett. , vol.431 , pp. 34-38
    • Darrouzet, E.1    Issartel, J.P.2    Lunardi, J.3    Dupuis, A.4
  • 37
    • 0035795163 scopus 로고    scopus 로고
    • Evidence for a quinone binding site close to the interface between NUOD and NUOB subunits of Complex I
    • I. Prieur, J. Lunardi, and A. Dupuis Evidence for a quinone binding site close to the interface between NUOD and NUOB subunits of Complex I Biochim. Biophys. Acta 1504 2001 173 178
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 173-178
    • Prieur, I.1    Lunardi, J.2    Dupuis, A.3
  • 39
    • 0043208847 scopus 로고    scopus 로고
    • Functional implications from an unexpected position of the 49 kDa subunit of complex I
    • V. Zickermann, M. Bostina, C. Hunte, T. Ruiz, M. Radermacher, and U. Brandt Functional implications from an unexpected position of the 49 kDa subunit of complex I J. Biol. Chem. 278 2003 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
  • 40
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • M. Ouali, and R.D. King Cascaded multiple classifiers for secondary structure prediction Protein Sci. 9 2000 1162 1176
    • (2000) Protein Sci. , vol.9 , pp. 1162-1176
    • Ouali, M.1    King, R.D.2
  • 41
    • 2442701768 scopus 로고    scopus 로고
    • Functional significance of conserved histidines and arginines in the 49 kDa subunit of mitochondrial complex I
    • L. Grgic, K. Zwicker, N. Kashani-Poor, S. Kerscher, and U. Brandt Functional significance of conserved histidines and arginines in the 49 kDa subunit of mitochondrial complex I J. Biol. Chem. 279 2004 21193 21199
    • (2004) J. Biol. Chem. , vol.279 , pp. 21193-21199
    • Grgic, L.1    Zwicker, K.2    Kashani-Poor, N.3    Kerscher, S.4    Brandt, U.5
  • 43
    • 0034663704 scopus 로고    scopus 로고
    • Application of the obligate aerobic yeast Yarrowia lipolytica as a eucaryotic model to analyze Leigh Syndrome mutations in the complex I core subunits PSST and TYKY
    • P. Ahlers, A. Garofano, S. Kerscher, and U. Brandt Application of the obligate aerobic yeast Yarrowia lipolytica as a eucaryotic model to analyze Leigh Syndrome mutations in the complex I core subunits PSST and TYKY Biochim. Biophys. Acta 1459 2000 258 265
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 258-265
    • Ahlers, P.1    Garofano, A.2    Kerscher, S.3    Brandt, U.4
  • 45
    • 0035918512 scopus 로고    scopus 로고
    • Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I)
    • T. Rasmussen, D. Scheide, B. Brors, L. Kintscher, H. Weiss, and T. Friedrich Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I) Biochemistry 40 2001 6124 6131
    • (2001) Biochemistry , vol.40 , pp. 6124-6131
    • Rasmussen, T.1    Scheide, D.2    Brors, B.3    Kintscher, L.4    Weiss, H.5    Friedrich, T.6
  • 48
    • 0025053384 scopus 로고
    • Cleavage-site motifs in mitochondrial targeting peptides
    • Y. Gavel, and G. von Heijne Cleavage-site motifs in mitochondrial targeting peptides Protein Eng. 4 1990 33 37
    • (1990) Protein Eng. , vol.4 , pp. 33-37
    • Gavel, Y.1    Von Heijne, G.2
  • 50
    • 0038497518 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation: Pitfalls and tips in measuring and interpreting enzyme activities
    • D. Chretien, and P. Rustin Mitochondrial oxidative phosphorylation: pitfalls and tips in measuring and interpreting enzyme activities J. Inherit. Metab. Dis. 26 2003 189 198
    • (2003) J. Inherit. Metab. Dis. , vol.26 , pp. 189-198
    • Chretien, D.1    Rustin, P.2
  • 51
    • 0038380689 scopus 로고    scopus 로고
    • Mitochondrial disorders: Clinical presentation and diagnostic dilemmas
    • J.A. Smeitink Mitochondrial disorders: clinical presentation and diagnostic dilemmas J. Inherit. Metab. Dis. 26 2004 199 207
    • (2004) J. Inherit. Metab. Dis. , vol.26 , pp. 199-207
    • Smeitink, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.