메뉴 건너뛰기




Volumn 20, Issue 1, 1999, Pages 79-87

Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes: Two enzymes are present in potato mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; CELL MEMBRANE; COMPLEMENTARY DNA; ENZYME BINDING; GENE DUPLICATION; MITOCHONDRION; MOLECULAR WEIGHT; PHYLOGENY; POTATO; PROTEIN TARGETING; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SOLUBILIZATION;

EID: 0033213361     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1999.00576.x     Document Type: Article
Times cited : (79)

References (40)
  • 1
    • 0026709336 scopus 로고
    • The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain
    • Braun, H.-P., Emmermann, M., Kruft, V. and Schmitz, U.K. (1992) The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J. 11,3219-3227.
    • (1992) EMBO J. , vol.11 , pp. 3219-3227
    • Braun, H.-P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 2
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by guanidiniumthiocyanate-phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N. (1987) Single-step method of RNA isolation by guanidiniumthiocyanate-phenol-chloroform extraction. Anal. Biochem. 167, 157-159.
    • (1987) Anal. Biochem. , vol.167 , pp. 157-159
    • Chomczynski, P.1    Sacchi, N.2
  • 4
    • 0015928859 scopus 로고
    • The external NADH dehydrogenases of intact plant mitochondria
    • Douce, R., Mannella, C.A. and Bonner, W.D. (1973) The external NADH dehydrogenases of intact plant mitochondria. Biochim. Biophys. Acta, 292, 105-116.
    • (1973) Biochim. Biophys. Acta , vol.292 , pp. 105-116
    • Douce, R.1    Mannella, C.A.2    Bonner, W.D.3
  • 5
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts
    • Friedrich, T., Steinmüller, K. and Weiss, H. (1995) The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Lett. 367, 107-111.
    • (1995) FEBS Lett. , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmüller, K.2    Weiss, H.3
  • 6
    • 0026463654 scopus 로고
    • The mitochondrial gene encoding ribosomal protein S12 has been translocated to the nuclear genome in Oenothera
    • Grohmann, L., Brennicke, A. and Schuster, W. (1992) The mitochondrial gene encoding ribosomal protein S12 has been translocated to the nuclear genome in Oenothera. Nucl. Acids Res. 20, 5641-5646.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 5641-5646
    • Grohmann, L.1    Brennicke, A.2    Schuster, W.3
  • 7
    • 0019403472 scopus 로고
    • Characterization of the respiratory NADH dehydrogenase of Escherichia coli and reconstitution of NADH oxidase in ndh mutant membrane vesicles
    • Jaworowski, A., Mayo, G., Shaw, D.C., Campbell, H.D. and Young, I.G. (1981) Characterization of the respiratory NADH dehydrogenase of Escherichia coli and reconstitution of NADH oxidase in ndh mutant membrane vesicles. Biochemistry, 20, 3621-3628.
    • (1981) Biochemistry , vol.20 , pp. 3621-3628
    • Jaworowski, A.1    Mayo, G.2    Shaw, D.C.3    Campbell, H.D.4    Young, I.G.5
  • 8
    • 0032472215 scopus 로고    scopus 로고
    • Rotenone-insensitive internal NADH-quinone 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. and Yagi, T. (1998) Rotenone-insensitive internal NADH-quinone 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. 421, 37-40.
    • (1998) FEBS Lett. , vol.421 , pp. 37-40
    • Kitajima-Ihara, T.1    Yagi, T.2
  • 9
    • 0028518882 scopus 로고
    • Tissue-specific differences of the mitochondrial protein import machinery: In vitro import, processing and degradation of the pre-F1β subunit of the ATP synthase in spinach leaf and root mitochondria
    • Knorpp, C., Hugosson, M., Sjöling, S., Eriksson, A.-C. and Glaser, E. (1994) Tissue-specific differences of the mitochondrial protein import machinery: in vitro import, processing and degradation of the pre-F1β subunit of the ATP synthase in spinach leaf and root mitochondria. Plant Mol. Biol. 26, 571-579.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 571-579
    • Knorpp, C.1    Hugosson, M.2    Sjöling, S.3    Eriksson, A.-C.4    Glaser, E.5
  • 10
    • 0028191673 scopus 로고
    • Purification, characterization, and submitochondrial localization of the 32-kilodalton NADH dehydrogenase from maize
    • Knudten, A.F., Thelen, J.J., Luethy, M.H. and Elthon, T.E. (1994) Purification, characterization, and submitochondrial localization of the 32-kilodalton NADH dehydrogenase from maize. Plant Physiol. 106, 1115-1122.
    • (1994) Plant Physiol. , vol.106 , pp. 1115-1122
    • Knudten, A.F.1    Thelen, J.J.2    Luethy, M.H.3    Elthon, T.E.4
  • 11
    • 0001898187 scopus 로고
    • Cloning and expression analysis of the plastidic fructose-1,6-bisphosphatase coding sequence from potato: Circumstantial evidence for the import of hexoses into chloroplasts
    • Koßmann, J., Müller-Röber, B., Dyer, T.A., Raines, C.A., Sonnewald, U. and Willmitzer, L. (1992) Cloning and expression analysis of the plastidic fructose-1,6-bisphosphatase coding sequence from potato: circumstantial evidence for the import of hexoses into chloroplasts. Planta, 188, 7-12.
    • (1992) Planta , vol.188 , pp. 7-12
    • Koßmann, J.1    Müller-Röber, B.2    Dyer, T.A.3    Raines, C.A.4    Sonnewald, U.5    Willmitzer, L.6
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0029562477 scopus 로고
    • NAD-binding domains of dehydrogenases
    • Lesk, A.M. (1995) NAD-binding domains of dehydrogenases. Curr. Biol. 5, 775-783.
    • (1995) Curr. Biol. , vol.5 , pp. 775-783
    • Lesk, A.M.1
  • 14
    • 0029105760 scopus 로고
    • Purification, characterization and submitochondrial localization of a 58-kilodalton NAD(P)H dehydrogenase
    • Luethy, M.H., Thelen, J.J., Knudten, A.F. and Elthon, T.E. (1995) Purification, characterization and submitochondrial localization of a 58-kilodalton NAD(P)H dehydrogenase. Plant Physiol. 107, 443-450.
    • (1995) Plant Physiol. , vol.107 , pp. 443-450
    • Luethy, M.H.1    Thelen, J.J.2    Knudten, A.F.3    Elthon, T.E.4
  • 15
    • 0032544505 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae nde1 and nde2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH
    • Lunik, M.A.H., Overkamp, K.M., Kötter, P., de Vries, S., van Dijken, P. and Pronk, J.T. (1998) The Saccharomyces cerevisiae nde1 and nde2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J. Biol. Chem. 273, 24529-24534.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24529-24534
    • Lunik, M.A.H.1    Overkamp, K.M.2    Kötter, P.3    De Vries, S.4    Van Dijken, P.5    Pronk, J.T.6
  • 16
    • 0025367420 scopus 로고
    • Calcium binding proteins. Elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments
    • Marsden, B.J., Shaw, G.S. and Sykes, B.D. (1990) Calcium binding proteins. Elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments. Biochem. Cell. Biol. 68, 587-601.
    • (1990) Biochem. Cell. Biol. , vol.68 , pp. 587-601
    • Marsden, B.J.1    Shaw, G.S.2    Sykes, B.D.3
  • 17
    • 0026089901 scopus 로고
    • Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH:ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae
    • Marres, C.A.M., de Vries, S. and Grivell, L.A. (1991) Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH:ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. Eur. J. Biochem. 195, 857-862.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 857-862
    • Marres, C.A.M.1    De Vries, S.2    Grivell, L.A.3
  • 18
    • 0030581482 scopus 로고    scopus 로고
    • Evidence for the presence of two rotenone-insensitive NAD(P)H dehydrogenases on the inner surface of the inner membrane of potato tuber mitochondria
    • Melo, A.M.P., Roberts, T.H. and Møller, I.M. (1996) Evidence for the presence of two rotenone-insensitive NAD(P)H dehydrogenases on the inner surface of the inner membrane of potato tuber mitochondria. Biochim. Biophys. Acta, 1276, 133-139.
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 133-139
    • Melo, A.M.P.1    Roberts, T.H.2    Møller, I.M.3
  • 19
    • 0030469323 scopus 로고    scopus 로고
    • Identification and characterisation of an inducible NAD(P)H dehydrogenase from red beetroot mitochondria
    • Menz, R.I. and Day, D.A. (1996) Identification and characterisation of an inducible NAD(P)H dehydrogenase from red beetroot mitochondria. Plant Physiol. 112, 607-613.
    • (1996) Plant Physiol. , vol.112 , pp. 607-613
    • Menz, R.I.1    Day, D.A.2
  • 20
    • 0030924730 scopus 로고    scopus 로고
    • The oxidation of cytosolic NAD(P)H by external NAD(P)H dehydrogenases in the respiratory chain of plant mitochondria
    • Møller, I.M. (1997) The oxidation of cytosolic NAD(P)H by external NAD(P)H dehydrogenases in the respiratory chain of plant mitochondria. Physiol. Plant. 100, 85-90.
    • (1997) Physiol. Plant. , vol.100 , pp. 85-90
    • Møller, I.M.1
  • 21
    • 0031952559 scopus 로고    scopus 로고
    • The role of NADP in the mitochondrial matrix
    • Møller, I.M. and Rasmusson, A.G. (1998) The role of NADP in the mitochondrial matrix. Trends Plant Sci. 3, 21-27.
    • (1998) Trends Plant Sci. , vol.3 , pp. 21-27
    • Møller, I.M.1    Rasmusson, A.G.2
  • 22
    • 0028674857 scopus 로고
    • Genes galore: A summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones
    • Newman, T., de Bruijn, F.J., Green, P. et al. (1994) Genes galore: a summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones. Plant Physiol. 106, 1241-1255.
    • (1994) Plant Physiol. , vol.106 , pp. 1241-1255
    • Newman, T.1    De Bruijn, F.J.2    Green, P.3
  • 23
    • 0028279520 scopus 로고
    • Prediction of transmembrane segments in proteins utilising multiple sequence alignments
    • Persson, B. and Argos, P. (1994) Prediction of transmembrane segments in proteins utilising multiple sequence alignments. J. Mol. Biol. 237, 182-192.
    • (1994) J. Mol. Biol. , vol.237 , pp. 182-192
    • Persson, B.1    Argos, P.2
  • 24
    • 0025932019 scopus 로고
    • Effect of calcium ions and inhibitors on internal NAD(P)H dehydrogenases in plant mitochondria
    • Rasmusson, A.G. and Møller, I.M. (1991) Effect of calcium ions and inhibitors on internal NAD(P)H dehydrogenases in plant mitochondria. Eur. J. Biochem. 202, 617-623.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 617-623
    • Rasmusson, A.G.1    Møller, I.M.2
  • 25
    • 0032053605 scopus 로고    scopus 로고
    • Characterisation of the 76kDa iron-sulphur protein subunit of plant mitochondrial complex I
    • Rasmusson, A.G., Heiser, V., Irrgang, K., Brennicke, A. and Grohmann, L. (1998a) Characterisation of the 76kDa iron-sulphur protein subunit of plant mitochondrial complex I. Plant Cell Physiol. 39, 373-381.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 373-381
    • Rasmusson, A.G.1    Heiser, V.2    Irrgang, K.3    Brennicke, A.4    Grohmann, L.5
  • 26
    • 0032490088 scopus 로고    scopus 로고
    • Physiological, biochemical and molecular aspects of mitochondrial complex I in plants
    • Rasmusson, A.G., Heiser, V., Zabaleta, E., Brennicke, A. and Grohmann, L. (1998b) Physiological, biochemical and molecular aspects of mitochondrial complex I in plants. Biochim. Biophys. Acta, 1364, 101-111.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 101-111
    • Rasmusson, A.G.1    Heiser, V.2    Zabaleta, E.3    Brennicke, A.4    Grohmann, L.5
  • 27
    • 0028862799 scopus 로고
    • Direct evidence for the presence of two external NAD(P)H dehydrogenases coupled to the electron transport chain in plant mitochondria
    • Roberts, T.H., Fredlund, K.M. and Møller, I.M. (1995) Direct evidence for the presence of two external NAD(P)H dehydrogenases coupled to the electron transport chain in plant mitochondria. FEBS Lett. 373, 307-309.
    • (1995) FEBS Lett. , vol.373 , pp. 307-309
    • Roberts, T.H.1    Fredlund, K.M.2    Møller, I.M.3
  • 29
    • 0031878085 scopus 로고    scopus 로고
    • Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae
    • Small, W.C. and McAlister-Henn, L. (1998) Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J. Bacteriol. 180, 4051-4055.
    • (1998) J. Bacteriol. , vol.180 , pp. 4051-4055
    • Small, W.C.1    McAlister-Henn, L.2
  • 30
    • 84989741846 scopus 로고
    • The presence of a short redox chain in the membrane of intact potato tuber peroxisomes and the association of malate dehydrogenase with the peroxisomal membrane
    • Struglics, A., Fredlund, K.M., Rasmusson, A.G. and Møller, I.M. (1993) The presence of a short redox chain in the membrane of intact potato tuber peroxisomes and the association of malate dehydrogenase with the peroxisomal membrane. Physiol. Plant. 88, 19-28.
    • (1993) Physiol. Plant. , vol.88 , pp. 19-28
    • Struglics, A.1    Fredlund, K.M.2    Rasmusson, A.G.3    Møller, I.M.4
  • 31
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne, G., Steppuhn, J. and Herrmann, R.G. (1989) Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180, 535-545.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 32
    • 0024288671 scopus 로고
    • Purification and characterisation of a rotenone-insensitive NADH-Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae
    • de Vries, S. and Grivell, L.A. (1988) Purification and characterisation of a rotenone-insensitive NADH-Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. Eur. J. Biochem. 176, 377-384.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 377-384
    • De Vries, S.1    Grivell, L.A.2
  • 33
    • 0023561970 scopus 로고
    • The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism
    • de Vries, S. and Marres, C.A.M. (1987) The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism. Biochim. Biophys. Acta, 895, 205-239.
    • (1987) Biochim. Biophys. Acta , vol.895 , pp. 205-239
    • De Vries, S.1    Marres, C.A.M.2
  • 34
    • 0026504047 scopus 로고
    • Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae
    • de Vries, S., van Witzenburg, R., Grivell, L.A. and Marres, C.A.M. (1992) Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. Eur. J. Biochem. 203, 587-592.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 587-592
    • De Vries, S.1    Van Witzenburg, R.2    Grivell, L.A.3    Marres, C.A.M.4
  • 35
    • 0031104941 scopus 로고    scopus 로고
    • Protein import into plant mitochondria
    • Whelan, J. and Glaser, E. (1997) Protein import into plant mitochondria. Plant Mol. Biol. 33, 771-789.
    • (1997) Plant Mol. Biol. , vol.33 , pp. 771-789
    • Whelan, J.1    Glaser, E.2
  • 36
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R.K., Terpstra, P. and Hol, W.G.J. (1986) Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187, 101-107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 37
    • 0029360329 scopus 로고
    • The formation of mRNA 3′-ends in plants
    • Wu, L., Ueda, T. and Messing, J. (1995) The formation of mRNA 3′-ends in plants. Plant J. 8, 323-329.
    • (1995) Plant J. , vol.8 , pp. 323-329
    • Wu, L.1    Ueda, T.2    Messing, J.3
  • 38
    • 0025908097 scopus 로고
    • Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1
    • Xu, X., Koyama, N., Cui, M., Yamagishi, A., Nosoh, Y. and Oshima, T. (1991) Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1. J. Biochem. 109, 678-683.
    • (1991) J. Biochem. , vol.109 , pp. 678-683
    • Xu, X.1    Koyama, N.2    Cui, M.3    Yamagishi, A.4    Nosoh, Y.5    Oshima, T.6
  • 39
    • 0025752593 scopus 로고
    • Bacterial NADH-quinone oxidoreductases
    • Yagi, T. (1991) Bacterial NADH-quinone oxidoreductases. J. Bioenerg. Biomembr. 23, 211-225.
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 211-225
    • Yagi, T.1
  • 40
    • 0019386665 scopus 로고
    • Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli
    • Young, I.G., Rogers, B.L., Campbell, H.D., Jaworowski, A. and Shaw, D.C. (1981) Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. Eur. J. Biochem. 116, 165-170.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 165-170
    • Young, I.G.1    Rogers, B.L.2    Campbell, H.D.3    Jaworowski, A.4    Shaw, D.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.