메뉴 건너뛰기




Volumn 48, Issue 4, 2010, Pages 265-272

Supramolecular structure of the OXPHOS system in highly thermogenic tissue of Arum maculatum

Author keywords

Alternative oxidase; Arum maculatum; Mitochondria; Oxidative phosphorylation; Respiratory supercomplexes; Thermogenesis

Indexed keywords

ALTERNATIVE OXIDASE; CYTOCHROME C OXIDASE; MULTIENZYME COMPLEX; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIQUINOL CYTOCHROME C REDUCTASE; VEGETABLE PROTEIN;

EID: 77949486574     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2010.01.010     Document Type: Article
Times cited : (21)

References (56)
  • 1
    • 0037116611 scopus 로고    scopus 로고
    • Exploring the molecular nature of alternative oxidase regulation and catalysis
    • Affourtit C., Albury M.S., Crichton P.G., and Moore A.L. Exploring the molecular nature of alternative oxidase regulation and catalysis. FEBS Lett. 510 (2002) 121-126
    • (2002) FEBS Lett. , vol.510 , pp. 121-126
    • Affourtit, C.1    Albury, M.S.2    Crichton, P.G.3    Moore, A.L.4
  • 2
    • 0037300778 scopus 로고    scopus 로고
    • Pollination ecology of Arum italicum (Araceae)
    • Albre J., Quilichini A., and Gibernau M. Pollination ecology of Arum italicum (Araceae). Bot. J. Linn. Soc. 141 (2003) 205-214
    • (2003) Bot. J. Linn. Soc. , vol.141 , pp. 205-214
    • Albre, J.1    Quilichini, A.2    Gibernau, M.3
  • 3
    • 0028896421 scopus 로고
    • Dynamics of thermogenesis and structure of epidermal tissue in the inflorescences of Arum maculatum
    • Bermadinger-Stabentheiner E., and Stabentheiner A. Dynamics of thermogenesis and structure of epidermal tissue in the inflorescences of Arum maculatum. New Phytol. 131 (1995) 41-50
    • (1995) New Phytol. , vol.131 , pp. 41-50
    • Bermadinger-Stabentheiner, E.1    Stabentheiner, A.2
  • 4
    • 33846968150 scopus 로고    scopus 로고
    • Supramolecular structure of the mitochondrial oxidative phosphorylation system
    • Boekema E.J., and Braun H.P. Supramolecular structure of the mitochondrial oxidative phosphorylation system. J. Biol. Chem. 282 (2007) 1-4
    • (2007) J. Biol. Chem. , vol.282 , pp. 1-4
    • Boekema, E.J.1    Braun, H.P.2
  • 5
    • 33845612757 scopus 로고    scopus 로고
    • Carbonic anhydrase subunits of the mitochondrial NADH dehydrogenase complex (complex I) in plants
    • Braun H.P., and Zabaleta E. Carbonic anhydrase subunits of the mitochondrial NADH dehydrogenase complex (complex I) in plants. Physiol. Plant 129 (2007) 114-122
    • (2007) Physiol. Plant , vol.129 , pp. 114-122
    • Braun, H.P.1    Zabaleta, E.2
  • 6
    • 0037431026 scopus 로고    scopus 로고
    • Identification of 14 new phosphoproteins involved in important plant mitochondrial processes
    • Bykova N.V., Egsgaard H., and Moller I.M. Identification of 14 new phosphoproteins involved in important plant mitochondrial processes. FEBS Lett. 540 (2003) 141-146
    • (2003) FEBS Lett. , vol.540 , pp. 141-146
    • Bykova, N.V.1    Egsgaard, H.2    Moller, I.M.3
  • 7
    • 4644250423 scopus 로고    scopus 로고
    • Higher plant-like subunit composition of mitochondrial complex I from Chlamydomonas reinhardtii: 31 conserved components among eukaryotes
    • Cardol P., Vanrobaeys F., Devreese B., Van Beeumen J., Matagne R.F., and Remacle C. Higher plant-like subunit composition of mitochondrial complex I from Chlamydomonas reinhardtii: 31 conserved components among eukaryotes. Biochim. Biophys. Acta 1658 (2004) 212-224
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 212-224
    • Cardol, P.1    Vanrobaeys, F.2    Devreese, B.3    Van Beeumen, J.4    Matagne, R.F.5    Remacle, C.6
  • 8
    • 0032077367 scopus 로고    scopus 로고
    • Changes in functional properties of mitochondria during growth cycle of Arabidopsis thaliana cell suspension cultures
    • De Virville J.D., Alin M.F., Aaron Y., Rémy R., Guillot-Salomon T., and Cantrel C. Changes in functional properties of mitochondria during growth cycle of Arabidopsis thaliana cell suspension cultures. Plant Physiol. Biochem. 36 (1998) 347-356
    • (1998) Plant Physiol. Biochem. , vol.36 , pp. 347-356
    • De Virville, J.D.1    Alin, M.F.2    Aaron, Y.3    Rémy, R.4    Guillot-Salomon, T.5    Cantrel, C.6
  • 10
    • 57049094966 scopus 로고    scopus 로고
    • The higher level of the oxidative phosphorylation system: mitochondrial supercomplexes
    • Dukina N.V., Sunderhaus S., Boekema E.J., and Braun H.P. The higher level of the oxidative phosphorylation system: mitochondrial supercomplexes. J. Bioenerg. Biomembr 40 (2008) 419-424
    • (2008) J. Bioenerg. Biomembr , vol.40 , pp. 419-424
    • Dukina, N.V.1    Sunderhaus, S.2    Boekema, E.J.3    Braun, H.P.4
  • 11
    • 0001335087 scopus 로고
    • Monoclonal antibodies to the alternative oxidase of higher plant mitochondria
    • Elthon T.E., Nickels R.L., and McIntosh L. Monoclonal antibodies to the alternative oxidase of higher plant mitochondria. Plant Physiol. 89 (1989) 1311-1317
    • (1989) Plant Physiol. , vol.89 , pp. 1311-1317
    • Elthon, T.E.1    Nickels, R.L.2    McIntosh, L.3
  • 12
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II
    • Eubel H., Jänsch L., and Braun H.P. New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II. Plant Physiol. 133 (2003) 274-286
    • (2003) Plant Physiol. , vol.133 , pp. 274-286
    • Eubel, H.1    Jänsch, L.2    Braun, H.P.3
  • 13
    • 1942501850 scopus 로고    scopus 로고
    • Identification and characterization of respirasomes in potato mitochondria
    • Eubel H., Heinemeyer J., and Braun H.P. Identification and characterization of respirasomes in potato mitochondria. Plant Physiol. 134 (2004) 1450-1459
    • (2004) Plant Physiol. , vol.134 , pp. 1450-1459
    • Eubel, H.1    Heinemeyer, J.2    Braun, H.P.3
  • 14
    • 33646478926 scopus 로고    scopus 로고
    • Pollination in the genus Arum - a review
    • Gibernau M., Macquart D., and Przetak G. Pollination in the genus Arum - a review. Aroideana 27 (2004) 148-166
    • (2004) Aroideana , vol.27 , pp. 148-166
    • Gibernau, M.1    Macquart, D.2    Przetak, G.3
  • 16
    • 0038433229 scopus 로고    scopus 로고
    • Mitochondrial complex I from Arabidopsis and rice: orthologs of mammalian and fungal components coupled with plant specific subunits
    • Heazlewood J.L., Howell K.A., and Millar A.H. Mitochondrial complex I from Arabidopsis and rice: orthologs of mammalian and fungal components coupled with plant specific subunits. Biochim. Biophys. Acta 1604 (2003) 159-169
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 159-169
    • Heazlewood, J.L.1    Howell, K.A.2    Millar, A.H.3
  • 17
    • 34249688217 scopus 로고    scopus 로고
    • A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria
    • Heinemeyer J., Braun H.P., Boekema E.J., and Kouril R. A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria. J. Biol. Chem. 282 (2007) 12240-12248
    • (2007) J. Biol. Chem. , vol.282 , pp. 12240-12248
    • Heinemeyer, J.1    Braun, H.P.2    Boekema, E.J.3    Kouril, R.4
  • 19
    • 0030111226 scopus 로고    scopus 로고
    • New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria
    • Jänsch L., Kruft V., Schmitz U.K., and Braun H.P. New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria. Plant J. 9 (1996) 357-368
    • (1996) Plant J. , vol.9 , pp. 357-368
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 20
    • 84979311350 scopus 로고
    • The respiration of Arum spadix. A rapid respiration, resistant to cyanide
    • James W.O., and Beevers H. The respiration of Arum spadix. A rapid respiration, resistant to cyanide. New Phytol. 49 (1950) 353-374
    • (1950) New Phytol. , vol.49 , pp. 353-374
    • James, W.O.1    Beevers, H.2
  • 21
    • 13244252296 scopus 로고    scopus 로고
    • The Holm Oak leaf proteome: analytical and biological variability in the protein expression level assessed by 2-DE and protein identification tandem mass spectrometry de novo sequencing and sequence similarity searching
    • Jorge I., Navarro R.M., Lenz C., Ariza D., Porras C., and Jorrín J. The Holm Oak leaf proteome: analytical and biological variability in the protein expression level assessed by 2-DE and protein identification tandem mass spectrometry de novo sequencing and sequence similarity searching. Proteomics 5 (2005) 222-234
    • (2005) Proteomics , vol.5 , pp. 222-234
    • Jorge, I.1    Navarro, R.M.2    Lenz, C.3    Ariza, D.4    Porras, C.5    Jorrín, J.6
  • 22
    • 0034669552 scopus 로고    scopus 로고
    • Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis
    • Jung C., Higgins C.M.J., and Xu Z. Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis. Anal. Biochem. 286 (2000) 214-223
    • (2000) Anal. Biochem. , vol.286 , pp. 214-223
    • Jung, C.1    Higgins, C.M.J.2    Xu, Z.3
  • 25
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial functions in Arabidopsis thaliana
    • Kruft V., Eubel H., Werhahn W., Jänsch L., and Braun H.P. Proteomic approach to identify novel mitochondrial functions in Arabidopsis thaliana. Plant Physiol. 127 (2001) 1694-1710
    • (2001) Plant Physiol. , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Werhahn, W.3    Jänsch, L.4    Braun, H.P.5
  • 26
    • 47849117424 scopus 로고    scopus 로고
    • Heterogeneity of the mitochondrial proteome for photosynthetic and non-photosynthetic Arabidopsis metabolism
    • Lee C.P., Eubel H., O'Toole N., and Millar A.H. Heterogeneity of the mitochondrial proteome for photosynthetic and non-photosynthetic Arabidopsis metabolism. Mol. Cell. Proteomics 7 (2008) 1297-1316
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1297-1316
    • Lee, C.P.1    Eubel, H.2    O'Toole, N.3    Millar, A.H.4
  • 27
    • 68949107623 scopus 로고    scopus 로고
    • Structural and functional organization of the mitochondrial respiratory chain: a dynamic super-assembly
    • Lenaz G., and Genova M.L. Structural and functional organization of the mitochondrial respiratory chain: a dynamic super-assembly. Int. J. Biochem. Cell Biol. 41 (2009) 1750-1772
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1750-1772
    • Lenaz, G.1    Genova, M.L.2
  • 28
    • 0027264668 scopus 로고
    • Organic acid activation of the alternative oxidase of plant mitochondria
    • Millar A.H., Wiskich J.T., Whelan J., and Day D.A. Organic acid activation of the alternative oxidase of plant mitochondria. FEBS Lett. 329 (1993) 259-262
    • (1993) FEBS Lett. , vol.329 , pp. 259-262
    • Millar, A.H.1    Wiskich, J.T.2    Whelan, J.3    Day, D.A.4
  • 29
    • 12344323931 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes contain plant specific subunits
    • Millar A.H., Eubel H., Jänsch L., Kruft V., Heazlewood J.L., and Braun H.P. Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes contain plant specific subunits. Plant Mol. Biol. 56 (2004) 77-90
    • (2004) Plant Mol. Biol. , vol.56 , pp. 77-90
    • Millar, A.H.1    Eubel, H.2    Jänsch, L.3    Kruft, V.4    Heazlewood, J.L.5    Braun, H.P.6
  • 30
    • 0022262821 scopus 로고
    • Clear background and highly sensitive protein staining with Coomassie blue dyes in polyacrylamide gels: a systematic analysis
    • Neuhoff V., Stamm R., and Eibl H. Clear background and highly sensitive protein staining with Coomassie blue dyes in polyacrylamide gels: a systematic analysis. Electrophoresis 6 (1985) 427-448
    • (1985) Electrophoresis , vol.6 , pp. 427-448
    • Neuhoff, V.1    Stamm, R.2    Eibl, H.3
  • 31
    • 0025320429 scopus 로고
    • Essential problems in quantification of proteins following colloidal staining with coomassie brilliant blue dyes in polyacrylamide gels, and their solution
    • Neuhoff V., Stamm R., Pardowitz I., Arold N., Ehrhardt W., and Taube D. Essential problems in quantification of proteins following colloidal staining with coomassie brilliant blue dyes in polyacrylamide gels, and their solution. Electrophoresis 11 (1990) 101-117
    • (1990) Electrophoresis , vol.11 , pp. 101-117
    • Neuhoff, V.1    Stamm, R.2    Pardowitz, I.3    Arold, N.4    Ehrhardt, W.5    Taube, D.6
  • 35
    • 37549064026 scopus 로고    scopus 로고
    • 2 supercomplex from Zea mays at 11-13 Å resolution: assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I
    • 2 supercomplex from Zea mays at 11-13 Å resolution: assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I. Biochim. Biophys. Acta 1777 (2008) 84-93
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 84-93
    • Peters, K.1    Dudkina, N.V.2    Jänsch, L.3    Braun, H.P.4    Boekema, E.J.5
  • 37
    • 0023656285 scopus 로고
    • Pyruvate transport by thermogenic-tissue mitochondria
    • Proudlove M.O., Beechey R.B., and Moore A.L. Pyruvate transport by thermogenic-tissue mitochondria. Biochem. J. 247 (1987) 441-447
    • (1987) Biochem. J. , vol.247 , pp. 441-447
    • Proudlove, M.O.1    Beechey, R.B.2    Moore, A.L.3
  • 38
    • 37249058385 scopus 로고    scopus 로고
    • The multiplicity of dehydrogenases in the electron transport chain of plant mitochondria
    • Rasmusson A.G., Geisler D.A., and Møller I.M. The multiplicity of dehydrogenases in the electron transport chain of plant mitochondria. Mitochondrion 8 (2008) 47-60
    • (2008) Mitochondrion , vol.8 , pp. 47-60
    • Rasmusson, A.G.1    Geisler, D.A.2    Møller, I.M.3
  • 39
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov L.A., and Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311 (2006) 1430-1436
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 41
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger H., and Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19 (2000) 1777-1783
    • (2000) EMBO J. , vol.19 , pp. 1777-1783
    • Schägger, H.1    Pfeiffer, K.2
  • 42
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., and Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Jagow, G.2
  • 43
    • 0035163149 scopus 로고    scopus 로고
    • Biophysics and physiology of temperature regulation in thermogenic flowers
    • Seymour R.S. Biophysics and physiology of temperature regulation in thermogenic flowers. Biosci. Rep. 21 (2001) 223-236
    • (2001) Biosci. Rep. , vol.21 , pp. 223-236
    • Seymour, R.S.1
  • 44
    • 0348227712 scopus 로고    scopus 로고
    • Thermogenesis and respiration of inflorescences of the dead horse arum Helicodiceros muscivorus, a pseudothermoregulatory aroid associated with fly pollination
    • Seymour R.S., Gibernau M., and Ito K. Thermogenesis and respiration of inflorescences of the dead horse arum Helicodiceros muscivorus, a pseudothermoregulatory aroid associated with fly pollination. Funct. Ecology 17 (2003) 886-894
    • (2003) Funct. Ecology , vol.17 , pp. 886-894
    • Seymour, R.S.1    Gibernau, M.2    Ito, K.3
  • 45
    • 0642367014 scopus 로고    scopus 로고
    • Heat reward for insect pollinators
    • Seymour R.S., White C.R., and Gibernau M. Heat reward for insect pollinators. Nature 426 (2003) 243-244
    • (2003) Nature , vol.426 , pp. 243-244
    • Seymour, R.S.1    White, C.R.2    Gibernau, M.3
  • 46
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm: a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov I.V., Seymour S.L., Patel A.A., Loboda A., Tang W.H., Keating S.P., Hunter C.L., Nuwaysir L.M., and Schaeffer D.A. The paragon algorithm: a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 6 (2007) 1638-1655
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 47
    • 0034663499 scopus 로고    scopus 로고
    • The mitochondrial cyanide resistant oxidase: structural conservation amid regulatory diversity
    • Siedow J.N., and Umbach A.L. The mitochondrial cyanide resistant oxidase: structural conservation amid regulatory diversity. Biochim. Biophys. Acta 1459 (2000) 432-439
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 432-439
    • Siedow, J.N.1    Umbach, A.L.2
  • 49
    • 0027140930 scopus 로고
    • Covalent and non-covalent dimers of the cyanide-resistant alternative oxidase protein in higher plant mitochondria and their relationship to enzyme activity
    • Umbach A.L., and Siedow J.N. Covalent and non-covalent dimers of the cyanide-resistant alternative oxidase protein in higher plant mitochondria and their relationship to enzyme activity. Plant Physiol. 103 (1993) 845-854
    • (1993) Plant Physiol. , vol.103 , pp. 845-854
    • Umbach, A.L.1    Siedow, J.N.2
  • 50
    • 51649125967 scopus 로고    scopus 로고
    • Proteomic analysis of Pinus radiata needles: 2-DE map and protein identification by LC/MS/MS and substitution-tolerant database searching
    • Valledor L., Castillejo M.A., Lenz C., Rodriguez R., Cañal M.J., and Jorrín J. Proteomic analysis of Pinus radiata needles: 2-DE map and protein identification by LC/MS/MS and substitution-tolerant database searching. J. Proteome Res. 7 (2008) 2616-2631
    • (2008) J. Proteome Res. , vol.7 , pp. 2616-2631
    • Valledor, L.1    Castillejo, M.A.2    Lenz, C.3    Rodriguez, R.4    Cañal, M.J.5    Jorrín, J.6
  • 52
    • 2442750218 scopus 로고    scopus 로고
    • In vivo ubiquinone reduction levels during thermogenesis in Araceae
    • Wagner A.M., Wagner M.J., and Moore A.L. In vivo ubiquinone reduction levels during thermogenesis in Araceae. Plant Physiol. 117 (1998) 1501-1506
    • (1998) Plant Physiol. , vol.117 , pp. 1501-1506
    • Wagner, A.M.1    Wagner, M.J.2    Moore, A.L.3
  • 53
    • 46349092784 scopus 로고    scopus 로고
    • Regulation of thermogenesis in flowering Araceae: the role of the alternative oxidase
    • Wagner A.M., Krab K., Wagner M.J., and Moore A.L. Regulation of thermogenesis in flowering Araceae: the role of the alternative oxidase. Biochim. Biophys. Acta 1777 (2008) 993-1000
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 993-1000
    • Wagner, A.M.1    Krab, K.2    Wagner, M.J.3    Moore, A.L.4
  • 54
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis thaliana: identification of multiple forms of TOM20
    • Werhahn W., Niemeyer A., Jänsch L., Kruft V., Schmitz U.K., and Braun H.P. Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis thaliana: identification of multiple forms of TOM20. Plant Physiol. 125 (2001) 943-954
    • (2001) Plant Physiol. , vol.125 , pp. 943-954
    • Werhahn, W.1    Niemeyer, A.2    Jänsch, L.3    Kruft, V.4    Schmitz, U.K.5    Braun, H.P.6
  • 56
    • 0030853263 scopus 로고    scopus 로고
    • Quantification of muscle mitochondria oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels
    • Zerbetto E., Verqani L., and Dabbeni-Sala F. Quantification of muscle mitochondria oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels. Electrophoresis 18 (1997) 2059-2064
    • (1997) Electrophoresis , vol.18 , pp. 2059-2064
    • Zerbetto, E.1    Verqani, L.2    Dabbeni-Sala, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.