메뉴 건너뛰기




Volumn 368, Issue 4, 2007, Pages 1114-1121

The External Alternative NAD(P)H Dehydrogenase NDE3 Is Localized both in the Mitochondria and in the Cytoplasm of Neurospora crassa

Author keywords

gene expression; mitochondria; NAD(P)H dehydrogenase; Neurospora crassa; respiratory mutant

Indexed keywords

GREEN FLUORESCENT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE;

EID: 34147171430     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.080     Document Type: Article
Times cited : (24)

References (49)
  • 1
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system. Annu. Rev. Biochem. 54 (1985) 1015-1069
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 2
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Moller I.M. Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52 (2001) 561-591
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Moller, I.M.1
  • 3
    • 0032588194 scopus 로고    scopus 로고
    • →H+/2e- stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles
    • Galkin A.S., Grivennikova V.G., and Vinogradov A.D. →H+/2e- stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles. FEBS Letters 451 (1999) 157-161
    • (1999) FEBS Letters , vol.451 , pp. 157-161
    • Galkin, A.S.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 4
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • Brandt U. Energy converting NADH:quinone oxidoreductase (complex I). Annu. Rev. Biochem. 75 (2006) 69-92
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 69-92
    • Brandt, U.1
  • 6
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker J.E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Quart. Rev. Biophys. 25 (1992) 253-324
    • (1992) Quart. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 7
    • 0034663640 scopus 로고    scopus 로고
    • Diversity and origin of alternative NADH:ubiquinone oxidoreductases
    • Kerscher S.J. 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.J.1
  • 8
    • 0037056054 scopus 로고    scopus 로고
    • From NADH to ubiquinone in Neurospora mitochondria
    • Videira A., and Duarte M. From NADH to ubiquinone in Neurospora mitochondria. Biochim. Biophys. Acta 1555 (2002) 187-191
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 187-191
    • Videira, A.1    Duarte, M.2
  • 9
    • 0027481581 scopus 로고
    • The bacterial energy-transducing NADH-quinone oxidoreductases
    • Yagi T. The bacterial energy-transducing NADH-quinone oxidoreductases. Biochim. Biophys. Acta 1141 (1993) 1-17
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 1-17
    • Yagi, T.1
  • 10
    • 0032812743 scopus 로고    scopus 로고
    • A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica
    • Kerscher S.J., Okun J.G., and Brandt U. 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.J.1    Okun, J.G.2    Brandt, U.3
  • 11
    • 0142152465 scopus 로고    scopus 로고
    • Arabidopsis genes encoding mitochondrial type II NAD(P)H dehydrogenases have different evolutionary origin and show distinct responses to light
    • Michalecka A.M., Svensson A.S., Johansson F.I., Agius S.C., Johanson U., Brennicke A., et al. Arabidopsis genes encoding mitochondrial type II NAD(P)H dehydrogenases have different evolutionary origin and show distinct responses to light. Plant Physiol. 133 (2003) 642-652
    • (2003) Plant Physiol. , vol.133 , pp. 642-652
    • Michalecka, A.M.1    Svensson, A.S.2    Johansson, F.I.3    Agius, S.C.4    Johanson, U.5    Brennicke, A.6
  • 12
    • 0037022830 scopus 로고    scopus 로고
    • Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: isolation and characterization
    • Fang J., and Beattie D.S. Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: isolation and characterization. Biochemistry 41 (2002) 3065-3072
    • (2002) Biochemistry , vol.41 , pp. 3065-3072
    • Fang, J.1    Beattie, D.S.2
  • 13
    • 2442543417 scopus 로고    scopus 로고
    • Respiratory metabolism: glycolysis, the TCA cycle and mitochondrial electron transport
    • Fernie A.R., Carrari F., and Sweetlove L.J. Respiratory metabolism: glycolysis, the TCA cycle and mitochondrial electron transport. Curr. Opin. Plant Biol. 7 (2004) 254-261
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 254-261
    • Fernie, A.R.1    Carrari, F.2    Sweetlove, L.J.3
  • 14
    • 0344064882 scopus 로고    scopus 로고
    • Beneficial interactions of mitochondrial metabolism with photosynthetic carbon assimilation
    • Raghavendra A.S., and Padmasree K. Beneficial interactions of mitochondrial metabolism with photosynthetic carbon assimilation. Trends Plant Sci. 8 (2003) 546-553
    • (2003) Trends Plant Sci. , vol.8 , pp. 546-553
    • Raghavendra, A.S.1    Padmasree, K.2
  • 15
    • 0037441390 scopus 로고    scopus 로고
    • External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide
    • Fang J., and Beattie D.S. External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide. Free Radic. Biol. Med. 34 (2003) 478-488
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 478-488
    • Fang, J.1    Beattie, D.S.2
  • 16
    • 33745377897 scopus 로고    scopus 로고
    • Yeast AMID homologue Ndi1p displays respiration-restricted apoptotic activity and is involved in chronological aging
    • Li W., Sun L., Liang Q., Wang J., Mo W., and Zhou B. Yeast AMID homologue Ndi1p displays respiration-restricted apoptotic activity and is involved in chronological aging. Mol. Biol. Cell 17 (2006) 1802-1811
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1802-1811
    • Li, W.1    Sun, L.2    Liang, Q.3    Wang, J.4    Mo, W.5    Zhou, B.6
  • 17
    • 33644867727 scopus 로고    scopus 로고
    • Reorganization of the alternative pathways of the Arabidopsis respiratory chain by nitrogen supply: opposing effects of ammonium and nitrate
    • Escobar M.A., Geisler D.A., and Rasmusson A.G. Reorganization of the alternative pathways of the Arabidopsis respiratory chain by nitrogen supply: opposing effects of ammonium and nitrate. Plant J. 45 (2006) 775-788
    • (2006) Plant J. , vol.45 , pp. 775-788
    • Escobar, M.A.1    Geisler, D.A.2    Rasmusson, A.G.3
  • 18
    • 0034782250 scopus 로고    scopus 로고
    • Light-dependent gene expression for proteins in the respiratory chain of potato leaves
    • Svensson A.S., and Rasmusson A.G. Light-dependent gene expression for proteins in the respiratory chain of potato leaves. Plant J. 28 (2001) 73-82
    • (2001) Plant J. , vol.28 , pp. 73-82
    • Svensson, A.S.1    Rasmusson, A.G.2
  • 19
    • 0024288671 scopus 로고
    • Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae
    • de Vries S., and Grivell L.A. Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. Eur. J. Biochem. 176 (1988) 377-384
    • (1988) Eur. J. Biochem. , vol.176 , pp. 377-384
    • de Vries, S.1    Grivell, L.A.2
  • 20
  • 21
    • 0032490105 scopus 로고    scopus 로고
    • Complex I from the fungus Neurospora crassa
    • Videira A. Complex I from the fungus Neurospora crassa. Biochim. Biophys. Acta 1364 (1998) 89-100
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 89-100
    • Videira, A.1
  • 22
    • 0035830925 scopus 로고    scopus 로고
    • The external calcium-dependent NADPH dehydrogenase from Neurospora crassa mitochondria
    • Melo A.M., Duarte M., Moller I.M., Prokisch H., Dolan P.L., Pinto L., et al. The external calcium-dependent NADPH dehydrogenase from Neurospora crassa mitochondria. J. Biol. Chem. 276 (2001) 3947-3951
    • (2001) J. Biol. Chem. , vol.276 , pp. 3947-3951
    • Melo, A.M.1    Duarte, M.2    Moller, I.M.3    Prokisch, H.4    Dolan, P.L.5    Pinto, L.6
  • 23
    • 1642533556 scopus 로고    scopus 로고
    • The main external alternative NAD(P)H dehydrogenase of Neurospora crassa mitochondria
    • Carneiro P., Duarte M., and Videira A. The main external alternative NAD(P)H dehydrogenase of Neurospora crassa mitochondria. Biochim. Biophys. Acta 1608 (2004) 45-52
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 45-52
    • Carneiro, P.1    Duarte, M.2    Videira, A.3
  • 24
    • 0038245247 scopus 로고    scopus 로고
    • The internal alternative NADH dehydrogenase of Neurospora crassa mitochondria
    • Duarte M., Peters M., Schulte U., and Videira A. The internal alternative NADH dehydrogenase of Neurospora crassa mitochondria. Biochem. J. 371 (2003) 1005-1011
    • (2003) Biochem. J. , vol.371 , pp. 1005-1011
    • Duarte, M.1    Peters, M.2    Schulte, U.3    Videira, A.4
  • 25
    • 0024276898 scopus 로고
    • Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein
    • Hawlitschek G., Schneider H., Schmidt B., Tropschug M., Hartl F.U., and Neupert W. Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein. Cell 53 (1988) 795-806
    • (1988) Cell , vol.53 , pp. 795-806
    • Hawlitschek, G.1    Schneider, H.2    Schmidt, B.3    Tropschug, M.4    Hartl, F.U.5    Neupert, W.6
  • 26
    • 0026541138 scopus 로고
    • Import of cytochrome c heme lyase into mitochondria: a novel pathway into the intermembrane space
    • Lill R., Stuart R.A., Drygas M.E., Nargang F.E., and Neupert W. Import of cytochrome c heme lyase into mitochondria: a novel pathway into the intermembrane space. EMBO J. 11 (1992) 449-456
    • (1992) EMBO J. , vol.11 , pp. 449-456
    • Lill, R.1    Stuart, R.A.2    Drygas, M.E.3    Nargang, F.E.4    Neupert, W.5
  • 27
    • 0024801086 scopus 로고
    • MOM19, an import receptor for mitochondrial precursor proteins
    • Sollner T., Griffiths G., Pfaller R., Pfanner N., and Neupert W. MOM19, an import receptor for mitochondrial precursor proteins. Cell 59 (1989) 1061-1070
    • (1989) Cell , vol.59 , pp. 1061-1070
    • Sollner, T.1    Griffiths, G.2    Pfaller, R.3    Pfanner, N.4    Neupert, W.5
  • 28
    • 13544262322 scopus 로고    scopus 로고
    • Competition of electrons to enter the respiratory chain: a new regulatory mechanism of oxidative metabolism in Saccharomyces cerevisiae
    • Bunoust O., Devin A., Averet N., Camougrand N., and Rigoulet M. Competition of electrons to enter the respiratory chain: a new regulatory mechanism of oxidative metabolism in Saccharomyces cerevisiae. J. Biol. Chem. 280 (2005) 3407-3413
    • (2005) J. Biol. Chem. , vol.280 , pp. 3407-3413
    • Bunoust, O.1    Devin, A.2    Averet, N.3    Camougrand, N.4    Rigoulet, M.5
  • 33
  • 34
    • 0029905931 scopus 로고    scopus 로고
    • Disruption of the nuclear gene encoding the 20.8-kDa subunit of NADH: ubiquinone reductase of Neurospora mitochondria
    • da Silva M.V., Alves P.C., Duarte M., Mota N., Lobo-da-Cunha A., Harkness T.A., et al. Disruption of the nuclear gene encoding the 20.8-kDa subunit of NADH: ubiquinone reductase of Neurospora mitochondria. Mol. Gen. Genet. 252 (1996) 177-183
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 177-183
    • da Silva, M.V.1    Alves, P.C.2    Duarte, M.3    Mota, N.4    Lobo-da-Cunha, A.5    Harkness, T.A.6
  • 35
    • 0020076852 scopus 로고
    • Properties of mitochondria as a function of the growth stages of Neurospora crassa
    • Schwitzguebel J.P., and Palmer J.M. Properties of mitochondria as a function of the growth stages of Neurospora crassa. J. Bacteriol. 149 (1982) 612-619
    • (1982) J. Bacteriol. , vol.149 , pp. 612-619
    • Schwitzguebel, J.P.1    Palmer, J.M.2
  • 36
    • 77956995235 scopus 로고
    • Genetic and microbiological research techniques for Neurospora crassa
    • Davis R.H., and de Serres F.J. Genetic and microbiological research techniques for Neurospora crassa. Methods Enzymol. 17A (1970) 79-143
    • (1970) Methods Enzymol. , vol.17 A , pp. 79-143
    • Davis, R.H.1    de Serres, F.J.2
  • 37
    • 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. Respiratory chain complex I is essential for sexual development in Neurospora and binding of iron sulfur clusters are required for enzyme assembly. Genetics 156 (2000) 607-615
    • (2000) Genetics , vol.156 , pp. 607-615
    • Duarte, M.1    Videira, A.2
  • 39
    • 4444362481 scopus 로고    scopus 로고
    • GFP as a tool to analyze the organization, dynamics and function of nuclei and microtubules in Neurospora crassa
    • Freitag M., Hickey P.C., Raju N.B., Selker E.U., and Read N.D. GFP as a tool to analyze the organization, dynamics and function of nuclei and microtubules in Neurospora crassa. Fungal Genet. Biol. 41 (2004) 897-910
    • (2004) Fungal Genet. Biol. , vol.41 , pp. 897-910
    • Freitag, M.1    Hickey, P.C.2    Raju, N.B.3    Selker, E.U.4    Read, N.D.5
  • 40
    • 0025641736 scopus 로고
    • Premeiotic instability of repeated sequences in Neurospora crassa
    • Selker E.U. Premeiotic instability of repeated sequences in Neurospora crassa. Annu. Rev. Genet. 24 (1990) 579-613
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 579-613
    • Selker, E.U.1
  • 41
    • 0024669082 scopus 로고
    • Assembly kinetics and identification of precursor proteins of complex I from Neurospora crassa
    • Videira A., and Werner S. Assembly kinetics and identification of precursor proteins of complex I from Neurospora crassa. Eur. J. Biochem. 181 (1989) 493-502
    • (1989) Eur. J. Biochem. , vol.181 , pp. 493-502
    • Videira, A.1    Werner, S.2
  • 44
    • 0000432497 scopus 로고    scopus 로고
    • Primary structure of a ferredoxin-like iron-sulfur subunit of complex I from Neurospora crassa
    • Duarte M., Finel M., and Videira A. Primary structure of a ferredoxin-like iron-sulfur subunit of complex I from Neurospora crassa. Biochim. Biophys. Acta 1275 (1996) 151-153
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 151-153
    • Duarte, M.1    Finel, M.2    Videira, A.3
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 47
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA 76 (1979) 4350-4354
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 48
    • 0032791402 scopus 로고    scopus 로고
    • Primary structure and characterisation of a 64 kDa NADH dehydrogenase from the inner membrane of Neurospora crassa mitochondria
    • Melo A.M., Duarte M., and Videira A. Primary structure and characterisation of a 64 kDa NADH dehydrogenase from the inner membrane of Neurospora crassa mitochondria. Biochim. Biophys. Acta 1412 (1999) 282-287
    • (1999) Biochim. Biophys. Acta , vol.1412 , pp. 282-287
    • Melo, A.M.1    Duarte, M.2    Videira, A.3
  • 49
    • 0025164244 scopus 로고
    • Nucleotide sequence of a full-length cDNA coding for the mitochondrial precursor protein of the beta-subunit of F1-ATPase from Neurospora crassa
    • Rassow J., Harmey M.A., Muller H.A., Neupert W., and Tropschug M. Nucleotide sequence of a full-length cDNA coding for the mitochondrial precursor protein of the beta-subunit of F1-ATPase from Neurospora crassa. Nucl. Acids Res. 18 (1990) 4922
    • (1990) Nucl. Acids Res. , vol.18 , pp. 4922
    • Rassow, J.1    Harmey, M.A.2    Muller, H.A.3    Neupert, W.4    Tropschug, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.