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Volumn 7, Issue , 2006, Pages

Loss of NAD(H) from swollen yeast mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; GLUTAMIC ACID; MALIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 33644873111     PISSN: 14712091     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-7-3     Document Type: Article
Times cited : (10)

References (36)
  • 1
    • 0031878085 scopus 로고    scopus 로고
    • Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae
    • Small WC, McAlister-Henn L: Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J Bacteriol 1998, 180:4051-4055.
    • (1998) J Bacteriol , vol.180 , pp. 4051-4055
    • Small, W.C.1    McAlister-Henn, L.2
  • 2
    • 0032544505 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH
    • Luttik MA, Overkamp KM, Kotter P, de Vries S, van Dijken JP, Pronk JT: The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 1998, 273:24529-24534.
    • (1998) J Biol Chem , vol.273 , pp. 24529-24534
    • Luttik, M.A.1    Overkamp, K.M.2    Kotter, P.3    De Vries, S.4    Van Dijken, J.P.5    Pronk, J.T.6
  • 3
    • 2442650104 scopus 로고    scopus 로고
    • Identification of the mitochondrial GTP/GDP transporter in Saccharomyces cerevisiae
    • Vozza A, Blanco E, Palmieri L, Palmieri F: Identification of the mitochondrial GTP/GDP transporter in Saccharomyces cerevisiae. J Biol Chem 2004, 279:20850-20857.
    • (2004) J Biol Chem , vol.279 , pp. 20850-20857
    • Vozza, A.1    Blanco, E.2    Palmieri, L.3    Palmieri, F.4
  • 4
    • 30744433627 scopus 로고    scopus 로고
    • Identification of the mitochondrial transporter for pyrimidine nucleotides in Saccharomyces cerevisiae: Bacterial expression, reconstitution and functional characterization
    • Marobbio CM, Di Noia MA, Palmieri F: Identification of the mitochondrial transporter for pyrimidine nucleotides in Saccharomyces cerevisiae: bacterial expression, reconstitution and functional characterization. Biochem J 2005.
    • (2005) Biochem J
    • Marobbio, C.M.1    Di Noia, M.A.2    Palmieri, F.3
  • 5
    • 0029984499 scopus 로고    scopus 로고
    • FLX1 codes for a carrier protein involved in maintaining a proper balance of flavin nucleotides in yeast mitochondria
    • Tzagoloff A, Jang J, Glerum DM, Wu M: FLX1 codes for a carrier protein involved in maintaining a proper balance of flavin nucleotides in yeast mitochondria. J Biol Chem 1996, 271:7392-7397.
    • (1996) J Biol Chem , vol.271 , pp. 7392-7397
    • Tzagoloff, A.1    Jang, J.2    Glerum, D.M.3    Wu, M.4
  • 6
    • 0035956859 scopus 로고    scopus 로고
    • The human mitochondrial deoxynucleotide carrier and its role in the toxicity of nucleoside antivirals
    • Dolce V, Fiermonte G, Runswick MJ, Palmieri F, Walker JE: The human mitochondrial deoxynucleotide carrier and its role in the toxicity of nucleoside antivirals. Proc Natl Acad Sci U S A 2001, 98:2284-2288.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2284-2288
    • Dolce, V.1    Fiermonte, G.2    Runswick, M.J.3    Palmieri, F.4    Walker, J.E.5
  • 7
    • 3142764629 scopus 로고    scopus 로고
    • Identification of the mitochondrial ATP-Mg/Pi transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution
    • Fiermonte G, De Leonardis F, Todisco S, Palmieri L, Lasorsa FM, Palmieri F: Identification of the mitochondrial ATP-Mg/Pi transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution. J Biol Chem 2004, 279:30722-30730.
    • (2004) J Biol Chem , vol.279 , pp. 30722-30730
    • Fiermonte, G.1    De Leonardis, F.2    Todisco, S.3    Palmieri, L.4    Lasorsa, F.M.5    Palmieri, F.6
  • 8
    • 0023449963 scopus 로고
    • cDNA sequence of a human skeletal muscle ADP/ATP translocator: Lack of a leader peptide, divergence from a fibroblast translocator cDNA, and coevolution with mitochondrial DNA genes
    • Neckelmann N, Li K, Wade RP, Shuster R, Wallace DC: cDNA sequence of a human skeletal muscle ADP/ATP translocator: lack of a leader peptide, divergence from a fibroblast translocator cDNA, and coevolution with mitochondrial DNA genes. Proc Natl Acad Sci U S A 1987, 84:7580-7584.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7580-7584
    • Neckelmann, N.1    Li, K.2    Wade, R.P.3    Shuster, R.4    Wallace, D.C.5
  • 10
    • 0021105306 scopus 로고
    • Slow passive diffusion of NAD+ between intact isolated plant mitochondria and suspending medium
    • Neuburger M, Douce R: Slow passive diffusion of NAD+ between intact isolated plant mitochondria and suspending medium. Biochem J 1983, 216:443-450.
    • (1983) Biochem J , vol.216 , pp. 443-450
    • Neuburger, M.1    Douce, R.2
  • 12
    • 0030826637 scopus 로고    scopus 로고
    • Properties of a cyclosporininsensitive permeability transition pore in yeast mitochondria
    • Jung DW, Bradshaw PC, Pfeiffer DR: Properties of a cyclosporininsensitive permeability transition pore in yeast mitochondria. J Biol Chem 1997, 272:21104-21112.
    • (1997) J Biol Chem , vol.272 , pp. 21104-21112
    • Jung, D.W.1    Bradshaw, P.C.2    Pfeiffer, D.R.3
  • 13
    • 0028052207 scopus 로고
    • ATP-induced unspecific channel in yeast mitochondria
    • Guerin B, Bunoust O, Rouqueys V, Rigoulet M: ATP-induced unspecific channel in yeast mitochondria. J Biol Chem 1994, 269:25406-25410.
    • (1994) J Biol Chem , vol.269 , pp. 25406-25410
    • Guerin, B.1    Bunoust, O.2    Rouqueys, V.3    Rigoulet, M.4
  • 14
    • 0031398232 scopus 로고    scopus 로고
    • Modulation of the electrophoretic ATP-induced K(+)-transport in yeast mitochondria by delta pH
    • Roucou X, Manon S, Guerin M: Modulation of the electrophoretic ATP-induced K(+)-transport in yeast mitochondria by delta pH. Biochem Mol Biol Int 1997, 43:53-61.
    • (1997) Biochem Mol Biol Int , vol.43 , pp. 53-61
    • Roucou, X.1    Manon, S.2    Guerin, M.3
  • 16
    • 0031039513 scopus 로고    scopus 로고
    • Conditions allowing different states of ATP- and GDP-induced permeability in mitochondria from different strains of Saccharomyces cerevisiae
    • Roucou X, Manon S, Guerin M: Conditions allowing different states of ATP- and GDP-induced permeability in mitochondria from different strains of Saccharomyces cerevisiae. Biochim Biophys Acta 1997, 1324:120-132.
    • (1997) Biochim Biophys Acta , vol.1324 , pp. 120-132
    • Roucou, X.1    Manon, S.2    Guerin, M.3
  • 17
    • 0032472215 scopus 로고    scopus 로고
    • Rotenone-insensitive internal NADHquinone oxidoreductase of Saccharomyces cerevisiae mitochondria: The enzyme expressed in Escherichia coli acts as a member of the respiratory chain in the host cells
    • Kitajima-Ihara T, Yagi T: Rotenone-insensitive internal NADHquinone oxidoreductase of Saccharomyces cerevisiae mitochondria: the enzyme expressed in Escherichia coli acts as a member of the respiratory chain in the host cells. FEBS Lett 1998, 421:37-40.
    • (1998) FEBS Lett , vol.421 , pp. 37-40
    • Kitajima-Ihara, T.1    Yagi, T.2
  • 18
    • 0032973114 scopus 로고    scopus 로고
    • Dependence of yeast mitochondrial unselective channel activity on the respiratory chain
    • Manon S: Dependence of yeast mitochondrial unselective channel activity on the respiratory chain. Biochim Biophys Acta 1999, 1410:85-90.
    • (1999) Biochim Biophys Acta , vol.1410 , pp. 85-90
    • Manon, S.1
  • 19
    • 7244224978 scopus 로고    scopus 로고
    • The human TAZ gene complements mitochondrial dysfunction in the yeast taz1Delta mutant. Implications for Barth syndrome
    • Ma L, Vaz FM, Gu Z, Wanders RJ, Greenberg ML: The human TAZ gene complements mitochondrial dysfunction in the yeast taz1Delta mutant. Implications for Barth syndrome. J Biol Chem 2004, 279:44394-44399.
    • (2004) J Biol Chem , vol.279 , pp. 44394-44399
    • Ma, L.1    Vaz, F.M.2    Gu, Z.3    Wanders, R.J.4    Greenberg, M.L.5
  • 20
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G, Guarente L: The Sir2 family of protein deacetylases. Annu Rev Biochem 2004, 73:417-435.
    • (2004) Annu Rev Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 21
    • 0026352171 scopus 로고
    • Differential sensitivity of the cellular compartments of Saccharomyces cerevisiae to protonophoric uncoupler under fermentative and respiratory energy supply
    • Beauvoit B, Rigoulet M, Raffard G, Canioni P, Guerin B: Differential sensitivity of the cellular compartments of Saccharomyces cerevisiae to protonophoric uncoupler under fermentative and respiratory energy supply. Biochemistry 1991, 30:11212-11220.
    • (1991) Biochemistry , vol.30 , pp. 11212-11220
    • Beauvoit, B.1    Rigoulet, M.2    Raffard, G.3    Canioni, P.4    Guerin, B.5
  • 22
    • 0027215424 scopus 로고
    • Interactions between glucose metabolism and oxidative phosphorylations on respiratory-competent Saccharomyces cerevisiae cells
    • Beauvoit B, Rigoulet M, Bunoust O, Raffard G, Canioni P, Guerin B: Interactions between glucose metabolism and oxidative phosphorylations on respiratory-competent Saccharomyces cerevisiae cells. Eur J Biochem 1993, 214:163-172.
    • (1993) Eur J Biochem , vol.214 , pp. 163-172
    • Beauvoit, B.1    Rigoulet, M.2    Bunoust, O.3    Raffard, G.4    Canioni, P.5    Guerin, B.6
  • 23
    • 0018906604 scopus 로고
    • Glucose repression and autolysis of Saccharomyces cerevisiae cells: Alterations in the cytochemical localization of acid phosphatase
    • Rainina EI, Zubatov AS, Luzikov VN: Glucose repression and autolysis of Saccharomyces cerevisiae cells: alterations in the cytochemical localization of acid phosphatase. Histochem J 1980, 12:57-69.
    • (1980) Histochem J , vol.12 , pp. 57-69
    • Rainina, E.I.1    Zubatov, A.S.2    Luzikov, V.N.3
  • 24
    • 0035831080 scopus 로고    scopus 로고
    • Pathophysiological relevance of mitochondria in NAD(+) metabolism
    • Di Lisa F, Ziegler M: Pathophysiological relevance of mitochondria in NAD(+) metabolism. FEBS Lett 2001, 492:4-8.
    • (2001) FEBS Lett , vol.492 , pp. 4-8
    • Di Lisa, F.1    Ziegler, M.2
  • 28
    • 0029848765 scopus 로고    scopus 로고
    • Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells
    • Zha H, Fisk HA, Yaffe MP, Mahajan N, Herman B, Reed JC: Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells. Mol Cell Biol 1996, 16:6494-6508.
    • (1996) Mol Cell Biol , vol.16 , pp. 6494-6508
    • Zha, H.1    Fisk, H.A.2    Yaffe, M.P.3    Mahajan, N.4    Herman, B.5    Reed, J.C.6
  • 31
    • 0018956403 scopus 로고
    • Pore size and properties of channels from mitochondria isolated from Neurospora crassa
    • Colombini M: Pore size and properties of channels from mitochondria isolated from Neurospora crassa. Journal of Membrane Biology 1980, 53:79-84.
    • (1980) Journal of Membrane Biology , vol.53 , pp. 79-84
    • Colombini, M.1
  • 32
    • 0035798599 scopus 로고    scopus 로고
    • Free fatty acids activate a vigorous Ca(2+):2H(+) antiport activity in yeast mitochondria
    • Bradshaw PC, Jung DW, Pfeiffer DR: Free fatty acids activate a vigorous Ca(2+):2H(+) antiport activity in yeast mitochondria. J Biol Chem 2001, 276:40502-40509.
    • (2001) J Biol Chem , vol.276 , pp. 40502-40509
    • Bradshaw, P.C.1    Jung, D.W.2    Pfeiffer, D.R.3
  • 33
    • 33644865074 scopus 로고    scopus 로고
    • Identification of the mitochondrial NAD+ transporter in Saccharomyces cerevisiae
    • Todisco S, Agrimi G, Castegna A, Palmieri F: Identification of the mitochondrial NAD+ transporter in Saccharomyces cerevisiae. J Biol Chem 2005.
    • (2005) J Biol Chem
    • Todisco, S.1    Agrimi, G.2    Castegna, A.3    Palmieri, F.4
  • 34
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum G, Bohni PC, Schatz G: Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J Biol Chem 1982, 257:13028-13033.
    • (1982) J Biol Chem , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 35
    • 0017201717 scopus 로고
    • Safranine as a probe of the mitochondrial membrane potential
    • Akerman KE, Wikstrom MK: Safranine as a probe of the mitochondrial membrane potential. FEBS Lett 1976, 68:191-197.
    • (1976) FEBS Lett , vol.68 , pp. 191-197
    • Akerman, K.E.1    Wikstrom, M.K.2
  • 36
    • 2442662845 scopus 로고    scopus 로고
    • Mitochondrial NADH redox state, monitoring discovery and deployment in tissue
    • Chance B: Mitochondrial NADH redox state, monitoring discovery and deployment in tissue. Methods Enzymol 2004, 385:361-370.
    • (2004) Methods Enzymol , vol.385 , pp. 361-370
    • Chance, B.1


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