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Volumn 9, Issue 10, 2010, Pages 2125-2139

Diurnal changes in mitochondrial function reveal daily optimization of light and dark respiratory metabolism in Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRATE AMINOTRANSFERASE; ELECTRON TRANSFERRING FLAVOPROTEIN; ENOYL COENZYME A HYDRATASE; FUMARATE HYDRATASE; MALATE DEHYDROGENASE; MITOCHONDRIAL PROTEIN; OXOGLUTARATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SUCCINATE DEHYDROGENASE; SUCCINIC SEMIALDEHYDE;

EID: 77957974224     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M110.001214     Document Type: Article
Times cited : (84)

References (98)
  • 1
    • 0000156704 scopus 로고
    • Models of integrated photosynthesis of cells and leaves
    • Farquhar, G. D. (1989) Models of integrated photosynthesis of cells and leaves. Philos. Trans. R. Soc. Lond. B Biol. Sci. 323, 357-367
    • (1989) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.323 , pp. 357-367
    • Farquhar, G.D.1
  • 2
    • 34250250163 scopus 로고
    • A biochemical model of photosynthetic CO2 assimilation in leaves of C-3 species
    • Farquhar, G. D., VonCaemmerer, S. V., and Berry, J. A. (1980) A biochemical model of photosynthetic CO2 assimilation in leaves of C-3 species. Planta 149, 78-90
    • (1980) Planta , vol.149 , pp. 78-90
    • Farquhar, G.D.1    VonCaemmerer, S.V.2    Berry, J.A.3
  • 3
    • 0030993514 scopus 로고    scopus 로고
    • Leaf respiration in light and darkness (a comparison of slow- and fast-growing Poa species)
    • Atkin, O. K., Westbeek, M., Cambridge, M. L., Lambers, H., and Pons, T. L. (1997) Leaf respiration in light and darkness (a comparison of slow- and fast-growing Poa species). Plant Physiol. 113, 961-965
    • (1997) Plant Physiol. , vol.113 , pp. 961-965
    • Atkin, O.K.1    Westbeek, M.2    Cambridge, M.L.3    Lambers, H.4    Pons, T.L.5
  • 4
    • 0001017693 scopus 로고
    • Regulation of respiration in the leaves and roots of two Lolium perenne populations with contrasting mature leaf respiration rates and crop yields
    • Day, D. A., De Vos, O. C., Wilson, D., and Lambers, H. (1985) Regulation of respiration in the leaves and roots of two Lolium perenne populations with contrasting mature leaf respiration rates and crop yields. Plant Physiol. 78, 678-683
    • (1985) Plant Physiol. , vol.78 , pp. 678-683
    • Day, D.A.1    De Vos, O.C.2    Wilson, D.3    Lambers, H.4
  • 5
    • 0034046580 scopus 로고    scopus 로고
    • Respiratory costs and rate of protein turnover in the roots of a fast-growing (Dactylis glomerata L.) and a slow-growing (Festuca ovina L.) grass species
    • Scheurwater, I., Dünnebacke, M., Eising, R., and Lambers, H. (2000) Respiratory costs and rate of protein turnover in the roots of a fast-growing (Dactylis glomerata L.) and a slow-growing (Festuca ovina L.) grass species. J. Exp. Bot. 51, 1089-1097 (Pubitemid 30343428)
    • (2000) Journal of Experimental Botany , vol.51 , Issue.347 , pp. 1089-1097
    • Scheurwater, I.1    Dunnebacke, M.2    Eising, R.3    Lambers, H.4
  • 6
    • 16644364005 scopus 로고    scopus 로고
    • Plant respiration and elevated atmospheric CO2 concentration: Cellular responses and global significance
    • Gonzalez-Meler, M. A., Taneva, L., and Trueman, R. J. (2004) Plant respiration and elevated atmospheric CO2 concentration: cellular responses and global significance. Ann. Bot. 94, 647-656
    • (2004) Ann. Bot. , vol.94 , pp. 647-656
    • Gonzalez-Meler, M.A.1    Taneva, L.2    Trueman, R.J.3
  • 7
    • 0347334397 scopus 로고
    • Light-induced development of glycine oxidation by mitochondria from sunflower cotyledons
    • Arron, G. P., and Edwards, G. E. (1980) Light-induced development of glycine oxidation by mitochondria from sunflower cotyledons. Plant Sci. Lett. 18, 229-235
    • (1980) Plant Sci. Lett. , vol.18 , pp. 229-235
    • Arron, G.P.1    Edwards, G.E.2
  • 8
    • 0022759684 scopus 로고
    • Light-induced increases in the glycine decarboxylase multienzyme complex from pea leaf mitochondria
    • Walker, J. L., and Oliver, D. J. (1986) Light-induced increases in the glycine decarboxylase multienzyme complex from pea leaf mitochondria. Arch. Biochem. Biophys. 248, 626-638
    • (1986) Arch. Biochem. Biophys. , vol.248 , pp. 626-638
    • Walker, J.L.1    Oliver, D.J.2
  • 9
    • 84989682260 scopus 로고
    • Glycine oxidation in mitochondria isolated from light grown and etiolated plant tissue
    • Lernmark, U., Henricson, D., Wigge, B., and Gardestrom, P. (1990) Glycine oxidation in mitochondria isolated from light grown and etiolated plant tissue. Physiol. Plant. 82, 339-344
    • (1990) Physiol. Plant. , vol.82 , pp. 339-344
    • Lernmark, U.1    Henricson, D.2    Wigge, B.3    Gardestrom, P.4
  • 10
    • 0028086766 scopus 로고
    • Interdependence of photosynthesis and respiration in plant cells - Interactions between chloroplasts and mitochondria
    • Raghavendra, A. S., Padmasree, K., and Saradadevi, K. (1994) Interdependence of photosynthesis and respiration in plant cells - interactions between chloroplasts and mitochondria. Plant Sci. 97, 1-14
    • (1994) Plant Sci. , vol.97 , pp. 1-14
    • Raghavendra, A.S.1    Padmasree, K.2    Saradadevi, K.3
  • 11
    • 0032494283 scopus 로고    scopus 로고
    • Interdependence between chloroplasts and mitochondria in the light and the dark
    • Hoefnagel, M. H., Atkin, O. K., and Wiskich, J. T. (1998) Interdependence between chloroplasts and mitochondria in the light and the dark. Biochim. Biophys. Acta 1366, 235-255
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 235-255
    • Hoefnagel, M.H.1    Atkin, O.K.2    Wiskich, J.T.3
  • 12
    • 0023002623 scopus 로고
    • Biochemical changes during sucrose deprivation in higher plant cells
    • Journet, E. P., Bligny, R., and Douce, R. (1986) Biochemical changes during sucrose deprivation in higher plant cells. J. Biol. Chem. 261, 3193-3199
    • (1986) J. Biol. Chem. , vol.261 , pp. 3193-3199
    • Journet, E.P.1    Bligny, R.2    Douce, R.3
  • 13
    • 0000149428 scopus 로고    scopus 로고
    • Induction of a carbon-starvation-related proteolysis in whole maize plants submitted to light/dark cycles and to extended darkness
    • Brouquisse, R., Gaudillere, J. P., and Raymond, P. (1998) Induction of a carbon-starvation-related proteolysis in whole maize plants submitted to light/dark cycles and to extended darkness. Plant Physiol. 117, 1281-1291
    • (1998) Plant Physiol. , vol.117 , pp. 1281-1291
    • Brouquisse, R.1    Gaudillere, J.P.2    Raymond, P.3
  • 16
    • 0031877829 scopus 로고    scopus 로고
    • Relationship between the inhibition of leaf respiration by light and enhancement of leaf dark respiration following light treatment
    • Atkin, O. K., Evans, J. R., and Siebke, K. (1998) Relationship between the inhibition of leaf respiration by light and enhancement of leaf dark respiration following light treatment. Aust. J. Plant Physiol. 25, 437-443
    • (1998) Aust. J. Plant Physiol. , vol.25 , pp. 437-443
    • Atkin, O.K.1    Evans, J.R.2    Siebke, K.3
  • 20
    • 0036246416 scopus 로고    scopus 로고
    • Essentiality of mitochondrial oxidative metabolism for photosynthesis: Optimization of carbon assimilation and protection against photoinhibition
    • Padmasree, K., Padmavathi, L., and Raghavendra, A. S. (2002) Essentiality of mitochondrial oxidative metabolism for photosynthesis: optimization of carbon assimilation and protection against photoinhibition. Crit. Rev. Biochem. Mol. Biol. 37, 71-119
    • (2002) Crit. Rev. Biochem. Mol. Biol. , vol.37 , pp. 71-119
    • Padmasree, K.1    Padmavathi, L.2    Raghavendra, A.S.3
  • 21
    • 70349638100 scopus 로고    scopus 로고
    • In folio respiratory fluxomics revealed by 13C isotopic labeling and H/D isotope effects highlight the noncyclic nature of the tricarboxylic acid "cycle" in illuminated leaves
    • Tcherkez, G., Mahé, A., Gauthier, P., Mauve, C., Gout, E., Bligny, R., Cornic, G., and Hodges, M. (2009) In folio respiratory fluxomics revealed by 13C isotopic labeling and H/D isotope effects highlight the noncyclic nature of the tricarboxylic acid "cycle" in illuminated leaves. Plant Physiol. 151, 620-630
    • (2009) Plant Physiol. , vol.151 , pp. 620-630
    • Tcherkez, G.1    Mahé, A.2    Gauthier, P.3    Mauve, C.4    Gout, E.5    Bligny, R.6    Cornic, G.7    Hodges, M.8
  • 22
    • 0027395918 scopus 로고
    • The organization and expression of the gene encoding the mitochondrial glycine decarboxylase complex and serine hydroxymethyltransferase in pea (Pisum sativum)
    • Turner, S. R., Hellens, R., Ireland, R., Ellis, N., and Rawsthorne, S. (1993) The organization and expression of the gene encoding the mitochondrial glycine decarboxylase complex and serine hydroxymethyltransferase in pea (Pisum sativum). Mol. Gen. Genet. 236, 402-408
    • (1993) Mol. Gen. Genet. , vol.236 , pp. 402-408
    • Turner, S.R.1    Hellens, R.2    Ireland, R.3    Ellis, N.4    Rawsthorne, S.5
  • 23
    • 0035979317 scopus 로고    scopus 로고
    • Multiple transcription-factor genes are early targets of phytochrome A signaling
    • Tepperman, J. M., Zhu, T., Chang, H. S., Wang, X., and Quail, P. H. (2001) Multiple transcription-factor genes are early targets of phytochrome A signaling. Proc. Natl. Acad. Sci. U.S.A. 98, 9437-9442
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9437-9442
    • Tepperman, J.M.1    Zhu, T.2    Chang, H.S.3    Wang, X.4    Quail, P.H.5
  • 24
    • 0034102077 scopus 로고    scopus 로고
    • Isolation and characterization of cDNA for the E1-beta and E2 subunits of the branched-chain alpha-ketoacid dehydrogenase complex in Arabidopsis
    • Fujiki, Y., Sato, T., Ito, M., and Watanabe, A. (2000) Isolation and characterization of cDNA for the E1-beta and E2 subunits of the branched-chain alpha-ketoacid dehydrogenase complex in Arabidopsis. J. Biol. Chem. 275, 6007-6013
    • (2000) J. Biol. Chem. , vol.275 , pp. 6007-6013
    • Fujiki, Y.1    Sato, T.2    Ito, M.3    Watanabe, A.4
  • 25
    • 33644688603 scopus 로고    scopus 로고
    • The critical role of Arabidopsis electron-transfer flavoprotein: ubiquinone oxidoreductase during dark-induced starvation
    • Ishizaki, K., Larson, T. R., Schauer, N., Fernie, A. R., Graham, I. A., and Leaver, C. J. (2005) The critical role of Arabidopsis electron-transfer flavoprotein:ubiquinone oxidoreductase during dark-induced starvation. Plant Cell 17, 2587-2600
    • (2005) Plant Cell , vol.17 , pp. 2587-2600
    • Ishizaki, K.1    Larson, T.R.2    Schauer, N.3    Fernie, A.R.4    Graham, I.A.5    Leaver, C.J.6
  • 26
    • 43149084126 scopus 로고    scopus 로고
    • NAD(H)-dependent glutamate dehydrogenase is essential for the survival of Arabidopsis thaliana during dark-induced carbon starvation
    • Miyashita, Y., and Good, A. G. (2008) NAD(H)-dependent glutamate dehydrogenase is essential for the survival of Arabidopsis thaliana during dark-induced carbon starvation. J. Exp. Bot. 59, 667-680
    • (2008) J. Exp. Bot. , vol.59 , pp. 667-680
    • Miyashita, Y.1    Good, A.G.2
  • 28
    • 33244470640 scopus 로고    scopus 로고
    • Characterization of mitochondrial alternative NAD(P)H dehydrogenases in Arabidopsis: Intraorganelle location and expression
    • Elhafez, D., Murcha, M. W., Clifton, R., Soole, K. L., Day, D. A., and Whelan, J. (2006) Characterization of mitochondrial alternative NAD(P)H dehydrogenases in Arabidopsis: intraorganelle location and expression. Plant Cell Physiol. 47, 43-54
    • (2006) Plant Cell Physiol. , vol.47 , pp. 43-54
    • Elhafez, D.1    Murcha, M.W.2    Clifton, R.3    Soole, K.L.4    Day, D.A.5    Whelan, J.6
  • 29
    • 33745390314 scopus 로고    scopus 로고
    • Transcript levels in plant mitochondria show a tight homeostasis during day and night
    • Okada, S., and Brennicke, A. (2006) Transcript levels in plant mitochondria show a tight homeostasis during day and night. Mol. Genet. Genomics 276, 71-78
    • (2006) Mol. Genet. Genomics , vol.276 , pp. 71-78
    • Okada, S.1    Brennicke, A.2
  • 30
    • 0345074089 scopus 로고    scopus 로고
    • Regulation of pyruvate dehydrogenase complex activity in plant cells
    • Tovar-Méndez, A., Miernyk, J. A., and Randall, D. D. (2003) Regulation of pyruvate dehydrogenase complex activity in plant cells. Eur. J. Biochem. 270, 1043-1049
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1043-1049
    • Tovar-Méndez, A.1    Miernyk, J.A.2    Randall, D.D.3
  • 32
    • 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. (2008) Heterogeneity of the mitochondrial proteome for photosynthetic and non-photosynthetic Arabidopsis metabolism. Mol. Cell. Proteomics 7, 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
  • 33
    • 84989673999 scopus 로고
    • Protein synthesis in mitochondria purified from roots, leaves and flowers of sugar beet
    • Lind, C., Hallden, C., and Moller, I. M. (1991) Protein synthesis in mitochondria purified from roots, leaves and flowers of sugar beet. Physiol. Plant. 83, 7-16
    • (1991) Physiol. Plant. , vol.83 , pp. 7-16
    • Lind, C.1    Hallden, C.2    Moller, I.M.3
  • 34
    • 0022135417 scopus 로고
    • Maize mitochondria synthesize organ-specific polypeptides
    • Newton, K. J., and Walbot, V. (1985) Maize mitochondria synthesize organ-specific polypeptides. Proc. Natl. Acad. Sci. U.S.A. 82, 6879-6883
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 6879-6883
    • Newton, K.J.1    Walbot, V.2
  • 35
    • 84988109731 scopus 로고
    • Analysis by two-dimensional gel electrophoresis of the polypeptide composition of pea mitochondria isolated from different tissues
    • Remy, R., Ambard-Bretteville, F., and Colas des Francs, C. (1987) Analysis by two-dimensional gel electrophoresis of the polypeptide composition of pea mitochondria isolated from different tissues. Electrophoresis 8, 528-532
    • (1987) Electrophoresis , vol.8 , pp. 528-532
    • Remy, R.1    Ambard-Bretteville, F.2    Colas Des Francs, C.3
  • 36
    • 84989709917 scopus 로고
    • Comparative electrophoretic studies of polypeptides in leaf, petiole and root mitochondria from spinach
    • Sachlstrom, S., and Ericson, I. (1984) Comparative electrophoretic studies of polypeptides in leaf, petiole and root mitochondria from spinach. Physiol. Plant. 61, 45-50
    • (1984) Physiol. Plant. , vol.61 , pp. 45-50
    • Sachlstrom, S.1    Ericson, I.2
  • 39
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner, F., Foster, L. J., Campanaro, S., Valle, G., and Mann, M. (2006) Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol. Cell. Proteomics 5, 608-619
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 41
    • 0000636038 scopus 로고
    • Biochemical characterization of chlorophyll-free mitochondria from pea leaves
    • Day, D. A., Neuburger, M., and Douce, R. (1985) Biochemical characterization of chlorophyll-free mitochondria from pea leaves. Aust. J. Plant Physiol. 12, 219-228
    • (1985) Aust. J. Plant Physiol. , vol.12 , pp. 219-228
    • Day, D.A.1    Neuburger, M.2    Douce, R.3
  • 43
    • 35448934538 scopus 로고    scopus 로고
    • Free flow electrophoresis for purification of plant mitochondria by surface charge
    • Eubel, H., Lee, C. P., Kuo, J., Meyer, E. H., Taylor, N. L., and Millar, A. H. (2007) Free flow electrophoresis for purification of plant mitochondria by surface charge. Plant J. 52, 583-594
    • (2007) Plant J. , vol.52 , pp. 583-594
    • Eubel, H.1    Lee, C.P.2    Kuo, J.3    Meyer, E.H.4    Taylor, N.L.5    Millar, A.H.6
  • 44
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silvered-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins from silvered-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 45
    • 0029010327 scopus 로고
    • Activation of glycine decarboxylase in pea leaf mitochondria by ATP
    • Zhang, Q., and Wiskich, J. T. (1995) Activation of glycine decarboxylase in pea leaf mitochondria by ATP. Arch. Biochem. Biophys. 320, 250-256
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 250-256
    • Zhang, Q.1    Wiskich, J.T.2
  • 46
    • 1342287231 scopus 로고    scopus 로고
    • Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis
    • Taylor, N. L., Heazlewood, J. L., Day, D. A., and Millar, A. H. (2004) Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis. Plant Physiol. 134, 838-848
    • (2004) Plant Physiol. , vol.134 , pp. 838-848
    • Taylor, N.L.1    Heazlewood, J.L.2    Day, D.A.3    Millar, A.H.4
  • 47
    • 0000165318 scopus 로고
    • Formate oxidation and oxygen reduction by leaf mitochondria
    • Oliver, D. J. (1981) Formate oxidation and oxygen reduction by leaf mitochondria. Plant Physiol. 68, 703-705
    • (1981) Plant Physiol. , vol.68 , pp. 703-705
    • Oliver, D.J.1
  • 49
    • 0017819382 scopus 로고
    • A simple spectrophotometric assay for fumarate hydratase in crude tissue extracts
    • Hatch, M. D. (1978) A simple spectrophotometric assay for fumarate hydratase in crude tissue extracts. Anal. Biochem. 85, 271-275
    • (1978) Anal. Biochem. , vol.85 , pp. 271-275
    • Hatch, M.D.1
  • 50
    • 0029767554 scopus 로고    scopus 로고
    • Purification of mitochondrial glutamate dehydrogenase from dark-grown soybean seedlings
    • Turano, F. J., Dashner, R., Upadhyaya, A., and Caldwell, C. R. (1996) Purification of mitochondrial glutamate dehydrogenase from dark-grown soybean seedlings. Plant Physiol. 112, 1357-1364
    • (1996) Plant Physiol. , vol.112 , pp. 1357-1364
    • Turano, F.J.1    Dashner, R.2    Upadhyaya, A.3    Caldwell, C.R.4
  • 51
    • 36549031664 scopus 로고    scopus 로고
    • Identification of intra- and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis
    • Winger, A. M., Taylor, N. L., Heazlewood, J. L., Day, D. A., and Millar, A. H. (2007) Identification of intra- and intermolecular disulphide bonding in the plant mitochondrial proteome by diagonal gel electrophoresis. Proteomics 7, 4158-4170
    • (2007) Proteomics , vol.7 , pp. 4158-4170
    • Winger, A.M.1    Taylor, N.L.2    Heazlewood, J.L.3    Day, D.A.4    Millar, A.H.5
  • 52
    • 33847104994 scopus 로고    scopus 로고
    • MascotDatfile: An open-source library to fully parse and analyse MASCOT MS/MS search results
    • Helsens, K., Martens, L., Vandekerckhove, J., and Gevaert, K. (2007) MascotDatfile: An open-source library to fully parse and analyse MASCOT MS/MS search results. Proteomics 7, 364-366
    • (2007) Proteomics , vol.7 , pp. 364-366
    • Helsens, K.1    Martens, L.2    Vandekerckhove, J.3    Gevaert, K.4
  • 53
    • 14744275289 scopus 로고    scopus 로고
    • Diurnal changes in the transcriptome encoding enzymes of starch metabolism provide evidence for both transcriptional and posttranscriptional regulation of starch metabolism in Arabidopsis leaves
    • Smith, S. M., Fulton, D. C., Chia, T., Thorneycroft, D., Chapple, A., Dunstan, H., Hylton, C., Zeeman, S. C., and Smith, A. M. (2004) Diurnal changes in the transcriptome encoding enzymes of starch metabolism provide evidence for both transcriptional and posttranscriptional regulation of starch metabolism in Arabidopsis leaves. Plant Physiol. 136, 2687-2699
    • (2004) Plant Physiol. , vol.136 , pp. 2687-2699
    • Smith, S.M.1    Fulton, D.C.2    Chia, T.3    Thorneycroft, D.4    Chapple, A.5    Dunstan, H.6    Hylton, C.7    Zeeman, S.C.8    Smith, A.M.9
  • 54
    • 33749120080 scopus 로고    scopus 로고
    • Integration of metabolite with transcript and enzyme activity profiling during diurnal cycles in Arabidopsis rosettes
    • Gibon, Y., Usadel, B., Blaesing, O. E., Kamlage, B., Hoehne, M., Trethewey, R., and Stitt, M. (2006) Integration of metabolite with transcript and enzyme activity profiling during diurnal cycles in Arabidopsis rosettes. Genome Biol. 7, R76
    • (2006) Genome Biol. , vol.7
    • Gibon, Y.1    Usadel, B.2    Blaesing, O.E.3    Kamlage, B.4    Hoehne, M.5    Trethewey, R.6    Stitt, M.7
  • 55
    • 33644872172 scopus 로고    scopus 로고
    • Antisense reduction of serine hydroxymethyltransferase results in diurnal displacement of NH4+ assimilation in leaves of Solanum tuberosum
    • Schjoerring, J. K., Mäck, G., Nielsen, K. H., Husted, S., Suzuki, A., Driscoll, S., Boldt, R., and Bauwe, H. (2006) Antisense reduction of serine hydroxymethyltransferase results in diurnal displacement of NH4+ assimilation in leaves of Solanum tuberosum. Plant J. 45, 71-82
    • (2006) Plant J. , vol.45 , pp. 71-82
    • Schjoerring, J.K.1    Mäck, G.2    Nielsen, K.H.3    Husted, S.4    Suzuki, A.5    Driscoll, S.6    Boldt, R.7    Bauwe, H.8
  • 56
    • 0034681906 scopus 로고    scopus 로고
    • Combined structural and biochemical analysis of the H-T complex in the glycine decarboxylase cycle: Evidence for a destabilization mechanism of the H-protein
    • Guilhaudis, L., Simorre, J. P., Blackledge, M., Marion, D., Gans, P., Neuburger, M., and Douce, R. (2000) Combined structural and biochemical analysis of the H-T complex in the glycine decarboxylase cycle: evidence for a destabilization mechanism of the H-protein. Biochemistry 39, 4259-4266
    • (2000) Biochemistry , vol.39 , pp. 4259-4266
    • Guilhaudis, L.1    Simorre, J.P.2    Blackledge, M.3    Marion, D.4    Gans, P.5    Neuburger, M.6    Douce, R.7
  • 58
    • 0038506859 scopus 로고    scopus 로고
    • Phosphorylation of formate dehydrogenase in potato tuber mitochondria
    • Bykova, N. V., Stensballe, A., Egsgaard, H., Jensen, O. N., and Moller, I. M. (2003) Phosphorylation of formate dehydrogenase in potato tuber mitochondria. J. Biol. Chem. 278, 26021-26030
    • (2003) J. Biol. Chem. , vol.278 , pp. 26021-26030
    • Bykova, N.V.1    Stensballe, A.2    Egsgaard, H.3    Jensen, O.N.4    Moller, I.M.5
  • 59
    • 0025139727 scopus 로고
    • Pea leaf mitochondrial pyruvate dehydrogenase complex is inactivated in vivo in a light-dependent manner
    • Budde, R. J., and Randall, D. D. (1990) Pea leaf mitochondrial pyruvate dehydrogenase complex is inactivated in vivo in a light-dependent manner. Proc. Natl. Acad. Sci. U.S.A. 87, 673-676
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 673-676
    • Budde, R.J.1    Randall, D.D.2
  • 60
    • 33747037187 scopus 로고    scopus 로고
    • The mitochondrial electron transfer flavoprotein complex is essential for survival of Arabidopsis in extended darkness
    • Ishizaki, K., Schauer, N., Larson, T. R., Graham, I. A., Fernie, A. R., and Leaver, C. J. (2006) The mitochondrial electron transfer flavoprotein complex is essential for survival of Arabidopsis in extended darkness. Plant J. 47, 751-760
    • (2006) Plant J. , vol.47 , pp. 751-760
    • Ishizaki, K.1    Schauer, N.2    Larson, T.R.3    Graham, I.A.4    Fernie, A.R.5    Leaver, C.J.6
  • 61
    • 33845628570 scopus 로고    scopus 로고
    • Fluctuations of gamma-aminobutyrate, gamma-hydroxybutyrate, and related amino acids in Arabidopsis leaves as a function of the light-dark cycle, leaf age, and N stress
    • Allan, W. L., and Shelp, B. J. (2006) Fluctuations of gamma-aminobutyrate, gamma-hydroxybutyrate, and related amino acids in Arabidopsis leaves as a function of the light-dark cycle, leaf age, and N stress. Can. J. Bot. 84, 1339-1346
    • (2006) Can. J. Bot. , vol.84 , pp. 1339-1346
    • Allan, W.L.1    Shelp, B.J.2
  • 62
    • 0036010137 scopus 로고    scopus 로고
    • Enzyme redundancy and the importance of 2-oxoglutarate in plant ammonium assimilation
    • Hodges, M. (2002) Enzyme redundancy and the importance of 2-oxoglutarate in plant ammonium assimilation. J. Exp. Bot. 53, 905-916
    • (2002) J. Exp. Bot. , vol.53 , pp. 905-916
    • Hodges, M.1
  • 64
    • 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. (2001) Light-dependent gene expression for proteins in the respiratory chain of potato leaves. Plant J. 28, 73-82
    • (2001) Plant J. , vol.28 , pp. 73-82
    • Svensson, A.S.1    Rasmusson, A.G.2
  • 65
  • 66
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft, V., Eubel, H., Jänsch, L., Werhahn, W., and Braun, H. P. (2001) Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol. 127, 1694-1710
    • (2001) Plant Physiol. , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jänsch, L.3    Werhahn, W.4    Braun, H.P.5
  • 67
  • 68
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • Heazlewood, J. L., Tonti-Filippini, J. S., Gout, A. M., Day, D. A., Whelan, J., and Millar, A. H. (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16, 241-256
    • (2004) Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 69
    • 60249086737 scopus 로고    scopus 로고
    • Experimental analysis of the rice mitochondrial proteome, its biogenesis, and heterogeneity
    • Huang, S., Taylor, N. L., Narsai, R., Eubel, H., Whelan, J., and Millar, A. H. (2009) Experimental analysis of the rice mitochondrial proteome, its biogenesis, and heterogeneity. Plant Physiol. 149, 719-734
    • (2009) Plant Physiol. , vol.149 , pp. 719-734
    • Huang, S.1    Taylor, N.L.2    Narsai, R.3    Eubel, H.4    Whelan, J.5    Millar, A.H.6
  • 71
    • 24044461712 scopus 로고    scopus 로고
    • Differential impact of environmental stresses on the pea mitochondrial proteome
    • Taylor, N. L., Heazlewood, J. L., Day, D. A., and Millar, A. H. (2005) Differential impact of environmental stresses on the pea mitochondrial proteome. Mol. Cell. Proteomics 4, 1122-1133
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1122-1133
    • Taylor, N.L.1    Heazlewood, J.L.2    Day, D.A.3    Millar, A.H.4
  • 72
    • 0000242111 scopus 로고
    • On the role of mitochondrial oxidative phosphorylation in photosynthesis metabolism as studied by the effect of oligomycin on photosynthesis in protoplasts and leaves of barley (Hordeum vulgare)
    • Krömer, S., and Heldt, H. W. (1991) On the role of mitochondrial oxidative phosphorylation in photosynthesis metabolism as studied by the effect of oligomycin on photosynthesis in protoplasts and leaves of barley (Hordeum vulgare). Plant Physiol. 95, 1270-1276
    • (1991) Plant Physiol. , vol.95 , pp. 1270-1276
    • Krömer, S.1    Heldt, H.W.2
  • 74
    • 0344064882 scopus 로고    scopus 로고
    • Beneficial interactions of mitochondrial metabolism with photosynthetic carbon assimilation
    • Raghavendra, A. S., and Padmasree, K. (2003) Beneficial interactions of mitochondrial metabolism with photosynthetic carbon assimilation. Trends Plant Sci. 8, 546-553
    • (2003) Trends Plant Sci. , vol.8 , pp. 546-553
    • Raghavendra, A.S.1    Padmasree, K.2
  • 75
    • 0037044794 scopus 로고    scopus 로고
    • Environmental stress causes oxidative damage to plant mitochondria leading to inhibition of glycine decarboxylase
    • Taylor, N. L., Day, D. A., and Millar, A. H. (2002) Environmental stress causes oxidative damage to plant mitochondria leading to inhibition of glycine decarboxylase. J. Biol. Chem. 277, 42663-42668
    • (2002) J. Biol. Chem. , vol.277 , pp. 42663-42668
    • Taylor, N.L.1    Day, D.A.2    Millar, A.H.3
  • 77
    • 21144436659 scopus 로고    scopus 로고
    • Mitochondrial aconitase is a transglutaminase 2 substrate: Transglutamination is a probable mechanism contributing to high-molecularweight aggregates of aconitase and loss of aconitase activity in Huntington disease brain
    • Kim, S. Y., Marekov, L., Bubber, P., Browne, S. E., Stavrovskaya, I., Lee, J., Steinert, P. M., Blass, J. P., Beal, M. F., Gibson, G. E., and Cooper, A. J. (2005) Mitochondrial aconitase is a transglutaminase 2 substrate: transglutamination is a probable mechanism contributing to high-molecularweight aggregates of aconitase and loss of aconitase activity in Huntington disease brain. Neurochem. Res. 30, 1245-1255
    • (2005) Neurochem. Res. , vol.30 , pp. 1245-1255
    • Kim, S.Y.1    Marekov, L.2    Bubber, P.3    Browne, S.E.4    Stavrovskaya, I.5    Lee, J.6    Steinert, P.M.7    Blass, J.P.8    Beal, M.F.9    Gibson, G.E.10    Cooper, A.J.11
  • 78
    • 0033794508 scopus 로고    scopus 로고
    • Impaired mitochondrial function results in increased tissue transglutaminase activity in situ
    • Lesort, M., Tucholski, J., Zhang, J., and Johnson, G. V. (2000) Impaired mitochondrial function results in increased tissue transglutaminase activity in situ. J. Neurochem. 75, 1951-1961
    • (2000) J. Neurochem. , vol.75 , pp. 1951-1961
    • Lesort, M.1    Tucholski, J.2    Zhang, J.3    Johnson, G.V.4
  • 79
    • 0028783872 scopus 로고
    • Degradation of the D1- and D2-proteins of photosystem II in higher plants is regulated by reversible phosphorylation
    • Koivuniemi, A., Aro, E. M., and Andersson, B. (1995) Degradation of the D1- and D2-proteins of photosystem II in higher plants is regulated by reversible phosphorylation. Biochemistry 34, 16022-16029
    • (1995) Biochemistry , vol.34 , pp. 16022-16029
    • Koivuniemi, A.1    Aro, E.M.2    Andersson, B.3
  • 80
    • 54349098202 scopus 로고    scopus 로고
    • Core protein phosphorylation facilitates the repair of photodamaged photosystem II at high light
    • Tikkanen, M., Nurmi, M., Kangasjärvi, S., and Aro, E. M. (2008) Core protein phosphorylation facilitates the repair of photodamaged photosystem II at high light. Biochim. Biophys. Acta 1777, 1432-1437
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1432-1437
    • Tikkanen, M.1    Nurmi, M.2    Kangasjärvi, S.3    Aro, E.M.4
  • 81
    • 0001719153 scopus 로고
    • Red light-induced accumulation of ubiquitin-phytochrome conjugates in both monocots and dicots
    • Jabben, M., Shanklin, J., and Vierstra, R. D. (1989) Red light-induced accumulation of ubiquitin-phytochrome conjugates in both monocots and dicots. Plant Physiol. 90, 380-384
    • (1989) Plant Physiol. , vol.90 , pp. 380-384
    • Jabben, M.1    Shanklin, J.2    Vierstra, R.D.3
  • 82
    • 3242776324 scopus 로고    scopus 로고
    • Identification of oxidised proteins in the matrix of rice leaf mitochondria by immunoprecipitation and two-dimensional liquid chromatography-tandem mass spectrometry
    • Kristensen, B. K., Askerlund, P., Bykova, N. V., Egsgaard, H., and Møller, I. M. (2004) Identification of oxidised proteins in the matrix of rice leaf mitochondria by immunoprecipitation and two-dimensional liquid chromatography-tandem mass spectrometry. Phytochemistry 65, 1839-1851
    • (2004) Phytochemistry , vol.65 , pp. 1839-1851
    • Kristensen, B.K.1    Askerlund, P.2    Bykova, N.V.3    Egsgaard, H.4    Møller, I.M.5
  • 83
    • 0242309094 scopus 로고    scopus 로고
    • Redox sensing and signalling associated with reactive oxygen in chloroplasts, peroxisomes and mitochondria
    • Foyer, C. H., and Noctor, G. (2003) Redox sensing and signalling associated with reactive oxygen in chloroplasts, peroxisomes and mitochondria. Physiol. Plant. 119, 355-364
    • (2003) Physiol. Plant. , vol.119 , pp. 355-364
    • Foyer, C.H.1    Noctor, G.2
  • 84
    • 0038705126 scopus 로고    scopus 로고
    • Leaf mitochondria modulate whole cell redox homeostasis, set antioxidant capacity, and determine stress resistance through altered signaling and diurnal regulation
    • Dutilleul, C., Garmier, M., Noctor, G., Mathieu, C., Chétrit, P., Foyer, C. H., and de Paepe, R. (2003) Leaf mitochondria modulate whole cell redox homeostasis, set antioxidant capacity, and determine stress resistance through altered signaling and diurnal regulation. Plant Cell 15, 1212-1226
    • (2003) Plant Cell , vol.15 , pp. 1212-1226
    • Dutilleul, C.1    Garmier, M.2    Noctor, G.3    Mathieu, C.4    Chétrit, P.5    Foyer, C.H.6    De Paepe, R.7
  • 85
    • 43049112810 scopus 로고    scopus 로고
    • No single way to understand singlet oxygen signalling in plants
    • Kim, C., Meskauskiene, R., Apel, K., and Laloi, C. (2008) No single way to understand singlet oxygen signalling in plants. EMBO Rep. 9, 435-439
    • (2008) EMBO Rep. , vol.9 , pp. 435-439
    • Kim, C.1    Meskauskiene, R.2    Apel, K.3    Laloi, C.4
  • 86
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, metabolism of reactive oxygen species
    • Moller, I. M. (2001) Plant mitochondria and oxidative stress: electron transport, NADPH turnover, metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 569-591
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 569-591
    • Moller, I.M.1
  • 87
    • 43549120312 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis
    • Heeg, C., Kruse, C., Jost, R., Gutensohn, M., Ruppert, T., Wirtz, M., and Hell, R. (2008) Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis. Plant Cell 20, 168-185
    • (2008) Plant Cell , vol.20 , pp. 168-185
    • Heeg, C.1    Kruse, C.2    Jost, R.3    Gutensohn, M.4    Ruppert, T.5    Wirtz, M.6    Hell, R.7
  • 88
    • 16844368306 scopus 로고    scopus 로고
    • The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress
    • Finkemeier, I., Goodman, M., Lamkemeyer, P., Kandlbinder, A., Sweetlove, L. J., and Dietz, K. J. (2005) The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress. J. Biol. Chem. 280, 12168-12180
    • (2005) J. Biol. Chem. , vol.280 , pp. 12168-12180
    • Finkemeier, I.1    Goodman, M.2    Lamkemeyer, P.3    Kandlbinder, A.4    Sweetlove, L.J.5    Dietz, K.J.6
  • 89
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • Chew, O., Whelan, J., and Millar, A. H. (2003) Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. J. Biol. Chem. 278, 46869-46877
    • (2003) J. Biol. Chem. , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 90
    • 33745630643 scopus 로고    scopus 로고
    • Inter-relationships between light and respiration in the control of ascorbic acid synthesis and accumulation in Arabidopsis thaliana leaves
    • Bartoli, C. G., Yu, J., Gómez, F., Fernández, L., McIntosh, L., and Foyer, C. H. (2006) Inter-relationships between light and respiration in the control of ascorbic acid synthesis and accumulation in Arabidopsis thaliana leaves. J. Exp. Bot. 57, 1621-1631
    • (2006) J. Exp. Bot. , vol.57 , pp. 1621-1631
    • Bartoli, C.G.1    Yu, J.2    Gómez, F.3    Fernández, L.4    McIntosh, L.5    Foyer, C.H.6
  • 92
    • 33745676828 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species. Contribution to oxidative stress and interorganellar signaling
    • Rhoads, D. M., Umbach, A. L., Subbaiah, C. C., and Siedow, J. N. (2006) Mitochondrial reactive oxygen species. Contribution to oxidative stress and interorganellar signaling. Plant Physiol. 141, 357-366
    • (2006) Plant Physiol. , vol.141 , pp. 357-366
    • Rhoads, D.M.1    Umbach, A.L.2    Subbaiah, C.C.3    Siedow, J.N.4
  • 93
    • 3242749880 scopus 로고    scopus 로고
    • Protein oxidation in plant mitochondria as a stress indicator
    • Moller, I. M., and Kristensen, B. K. (2004) Protein oxidation in plant mitochondria as a stress indicator. Photochem. Photobiol. Sci. 3, 730-735
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 730-735
    • Moller, I.M.1    Kristensen, B.K.2
  • 94
    • 0001547226 scopus 로고
    • 2 uptake) in leaves - Measurement, environmental dependencies, and kinetic properties
    • 2 uptake) in leaves - measurement, environmental dependencies, and kinetic properties. Plant Physiol. 76, 723-729
    • (1984) Plant Physiol. , vol.76 , pp. 723-729
    • Laisk, A.1    Kiirats, O.2    Oja, V.3
  • 95
    • 0027132883 scopus 로고
    • On the function of mitochondrial metabolism during photosynthesis in spinach (Spinacia oleracea L.) leaves. (Partitioning between respiration and export of redox equivalents and precursors for nitrate assimilation products)
    • Hanning, I., and Heldt, H. W. (1993) On the function of mitochondrial metabolism during photosynthesis in spinach (Spinacia oleracea L.) leaves. (Partitioning between respiration and export of redox equivalents and precursors for nitrate assimilation products). Plant Physiol. 103, 1147-1154
    • (1993) Plant Physiol. , vol.103 , pp. 1147-1154
    • Hanning, I.1    Heldt, H.W.2
  • 96
    • 0344530381 scopus 로고    scopus 로고
    • Reduced expression of aconitase results in an enhanced rate of photosynthesis and marked shifts in carbon partitioning in illuminated leaves of wild species tomato
    • Carrari, F., Nunes-Nesi, A., Gibon, Y., Lytovchenko, A., Loureiro, M. E., and Fernie, A. R. (2003) Reduced expression of aconitase results in an enhanced rate of photosynthesis and marked shifts in carbon partitioning in illuminated leaves of wild species tomato. Plant Physiol. 133, 1322-1335
    • (2003) Plant Physiol. , vol.133 , pp. 1322-1335
    • Carrari, F.1    Nunes-Nesi, A.2    Gibon, Y.3    Lytovchenko, A.4    Loureiro, M.E.5    Fernie, A.R.6
  • 97
    • 0035983636 scopus 로고    scopus 로고
    • Metabolic and environmental regulation of 3-methylcrotonyl-coenzyme A carboxylase expression in Arabidopsis
    • Che, P., Wurtele, E. S., and Nikolau, B. J. (2002) Metabolic and environmental regulation of 3-methylcrotonyl-coenzyme A carboxylase expression in Arabidopsis. Plant Physiol. 129, 625-637
    • (2002) Plant Physiol. , vol.129 , pp. 625-637
    • Che, P.1    Wurtele, E.S.2    Nikolau, B.J.3
  • 98
    • 0037636431 scopus 로고    scopus 로고
    • Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants
    • Bouché, N., Fait, A., Bouchez, D., Møller, S. G., and Fromm, H. (2003) Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants. Proc. Natl. Acad. Sci. U.S.A. 100, 6843-6848
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6843-6848
    • Bouché, N.1    Fait, A.2    Bouchez, D.3    Møller, S.G.4    Fromm, H.5


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