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Volumn 21, Issue 2, 2003, Pages 133-144

Identification of mitochondrial protein complexes in arabidopsis using two-dimensional blue-native polyacrylamide gel electrophoresis

Author keywords

Blue native; Mass spectrometry; Plant mitochondria; Protein complexes; Proteomic

Indexed keywords

ARABIDOPSIS; EMBRYOPHYTA;

EID: 0041379444     PISSN: 07359640     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02774240     Document Type: Article
Times cited : (27)

References (45)
  • 1
    • 0037127260 scopus 로고    scopus 로고
    • Occurrence and characteristics of the mitochondrial permeability transition in plants
    • Arpagaus S, Rawyler A, and Braendle R (2002) Occurrence and characteristics of the mitochondrial permeability transition in plants. J Biol Chem 277: 1780-1787.
    • (2002) J Biol Chem , vol.277 , pp. 1780-1787
    • Arpagaus, S.1    Rawyler, A.2    Braendle, R.3
  • 2
    • 0033408491 scopus 로고    scopus 로고
    • Translocation of cytochrome c from the mitochondria to the cytosol occurs during heat-induced programmed cell death in cucumber plants
    • Balk J, Leaver CJ, and McCabe PF (1999) Translocation of cytochrome c from the mitochondria to the cytosol occurs during heat-induced programmed cell death in cucumber plants. FEBS Lett 463: 151-154.
    • (1999) FEBS Lett , vol.463 , pp. 151-154
    • Balk, J.1    Leaver, C.J.2    McCabe, P.F.3
  • 5
    • 0033198449 scopus 로고    scopus 로고
    • The protein-import apparatus of plant mitochondria
    • Braun HP and Schmitz UK (1999) The protein-import apparatus of plant mitochondria. Planta 209: 267-274.
    • (1999) Planta , vol.209 , pp. 267-274
    • Braun, H.P.1    Schmitz, U.K.2
  • 6
    • 0032422634 scopus 로고    scopus 로고
    • The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition
    • Brdiczka D, Beutner G, Ruck A, Dolder M, and Wallimann T (1998) The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition. Biofactors 8: 235-242.
    • (1998) Biofactors , vol.8 , pp. 235-242
    • Brdiczka, D.1    Beutner, G.2    Ruck, A.3    Dolder, M.4    Wallimann, T.5
  • 8
    • 0036668515 scopus 로고    scopus 로고
    • High throughput two-dimensional blue-native electrophoresis: A tool for functional proteomics of mitochondria and signalling complexes
    • Brookes S, Pinner A, Ramachandran A, Coward L, Barnes S, Kim H, and Darley-Usmar VM (2002) High throughput two-dimensional blue-native electrophoresis: a tool for functional proteomics of mitochondria and signalling complexes. Proteomics 2: 969-977.
    • (2002) Proteomics , vol.2 , pp. 969-977
    • Brookes, S.1    Pinner, A.2    Ramachandran, A.3    Coward, L.4    Barnes, S.5    Kim, H.6    Darley-Usmar, V.M.7
  • 10
    • 0027135082 scopus 로고
    • Ketol-Acid Reductoisomerase from Barley (Hordeum vulgare) Purification, Properties, and Specific Inhibition
    • Durner J, Knorzer OC, and Boger P (1993) Ketol-Acid Reductoisomerase from Barley (Hordeum vulgare) Purification, Properties, and Specific Inhibition. Plant Physiol 103: 903-910.
    • (1993) Plant Physiol , vol.103 , pp. 903-910
    • Durner, J.1    Knorzer, O.C.2    Boger, P.3
  • 11
    • 0028214871 scopus 로고
    • The C-terminus of the 14-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae is involved in the assembly of a functional enzyme
    • Hemrika W, De Jong M, Berden JA, and Grivell LA (1994) The C-terminus of the 14-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae is involved in the assembly of a functional enzyme. Eur J Biochem 220: 569-576.
    • (1994) Eur J Biochem , vol.220 , pp. 569-576
    • Hemrika, W.1    De Jong, M.2    Berden, J.A.3    Grivell, L.A.4
  • 12
    • 85039503001 scopus 로고    scopus 로고
    • GARNet Web site. 1 June
    • Genomic Arabidopsis Resource Network. GARNet Web site. 1 June 2003 〈http://spare0.york.ac.uk/res/gamet/gamet.htm〉.
    • (2003)
  • 13
    • 0034913239 scopus 로고    scopus 로고
    • The origin and early evolution of mitochondria
    • Reviews 1018
    • Gray MW, Burger G, and Lang BF (2001) The origin and early evolution of mitochondria. Genome Biol 2: Reviews 1018.
    • (2001) Genome Biol , vol.2
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 14
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR and Reed JC (1998) Mitochondria and apoptosis. Science 281: 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 15
    • 0034681334 scopus 로고    scopus 로고
    • Fatty acid and lipoic acid biosynthesis in higher plant mitochondria
    • Gueguen V, Macherel D, Jaquinod M, Douce R, and Bourguignon J (2000) Fatty acid and lipoic acid biosynthesis in higher plant mitochondria. J Biol Chem 275: 5016-5025.
    • (2000) J Biol Chem , vol.275 , pp. 5016-5025
    • Gueguen, V.1    Macherel, D.2    Jaquinod, M.3    Douce, R.4    Bourguignon, J.5
  • 16
    • 0030111226 scopus 로고    scopus 로고
    • New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria
    • Jansch L, Kruft V, Schmitz UK, and Braun HP (1996) New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria. Plant J 9: 357-368.
    • (1996) Plant J , vol.9 , pp. 357-368
    • Jansch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 17
    • 0024115612 scopus 로고
    • Structural organization of glutamate dehydrogenase hexamer. 1. Immobilization on sepharose as a model for analysis of structural-functional characteristics of the enzyme
    • Karabashian LV, Agadzhanian SA, Danoian KV, and Kazarian RA (1988) Structural organization of glutamate dehydrogenase hexamer. 1. Immobilization on sepharose as a model for analysis of structural-functional characteristics of the enzyme. Bioorg Khim 14: 1495-1501.
    • (1988) Bioorg Khim , vol.14 , pp. 1495-1501
    • Karabashian, L.V.1    Agadzhanian, S.A.2    Danoian, K.V.3    Kazarian, R.A.4
  • 18
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft V, Eubel H, Jansch L, Werhahn W, and Braun HP (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    Jansch, L.3    Werhahn, W.4    Braun, H.P.5
  • 19
    • 0031055338 scopus 로고    scopus 로고
    • Molecular chaperones and mitochondrial protein folding
    • Martin J (1997) Molecular chaperones and mitochondrial protein folding. J Bioenerg Biomembr 29: 35-43.
    • (1997) J Bioenerg Biomembr , vol.29 , pp. 35-43
    • Martin, J.1
  • 20
    • 0023038384 scopus 로고
    • Subunit equilibria of porcine heart citrate synthase. Effects of enzyme concentration, pH, and substrates
    • McEvily AJ and Harrison JH (1986) Subunit equilibria of porcine heart citrate synthase. Effects of enzyme concentration, pH, and substrates. J Biol Chem 261: 2593-2598.
    • (1986) J Biol Chem , vol.261 , pp. 2593-2598
    • McEvily, A.J.1    Harrison, J.H.2
  • 21
    • 0032750542 scopus 로고    scopus 로고
    • Higher plant mitochondria
    • Mackenzie S and McIntosh L (1999) Higher plant mitochondria. Plant Cell 11: 571-586.
    • (1999) Plant Cell , vol.11 , pp. 571-586
    • Mackenzie, S.1    McIntosh, L.2
  • 22
    • 0033569439 scopus 로고    scopus 로고
    • Plant mitochondrial 2-oxoglutarate dehydrogenase complex: Purification and characterization in potato
    • Millar AH, Hill SA, and Leaver CJ (1999) Plant mitochondrial 2-oxoglutarate dehydrogenase complex: purification and characterization in potato. Biochem J 343: 327-334.
    • (1999) Biochem J , vol.343 , pp. 327-334
    • Millar, A.H.1    Hill, S.A.2    Leaver, C.J.3
  • 24
    • 0031952559 scopus 로고    scopus 로고
    • The role of NADP in the mitochondrial matrix
    • Moller IM and Rasmusson AG (1998) The role of NADP in the mitochondrial matrix. Trends Plant Sci 3: 21-27.
    • (1998) Trends Plant Sci , vol.3 , pp. 21-27
    • Moller, I.M.1    Rasmusson, A.G.2
  • 26
    • 85039486311 scopus 로고    scopus 로고
    • Matrix Science Web site. 5 May
    • Matrix Science Inc. Matrix Science Web site. 5 May 2003 〈http://www.matiixscience.com〉.
    • (2003)
  • 27
    • 0027143463 scopus 로고
    • Oxidative Stimulation of Glutathione Synthesis in Arabidopsis thaliana Suspension Cultures
    • May MJ and Leaver CJ (1993) Oxidative Stimulation of Glutathione Synthesis in Arabidopsis thaliana Suspension Cultures. Plant Physiol 103: 621-627.
    • (1993) Plant Physiol , vol.103 , pp. 621-627
    • May, M.J.1    Leaver, C.J.2
  • 28
    • 85039494852 scopus 로고    scopus 로고
    • Waters Mass Spectrometry Systems Micromass Web site. 1 June
    • Micromass. Waters Mass Spectrometry Systems Micromass Web site. 1 June 2003 〈http://www.micromass.co.uk〉.
    • (2003)
  • 29
    • 0025091802 scopus 로고
    • Biogenesis of mitochondrial porin: The import pathway
    • Pfaller R, Kleene R, and Neupert W (1990) Biogenesis of mitochondrial porin: the import pathway. Experientia 46: 153-161.
    • (1990) Experientia , vol.46 , pp. 153-161
    • Pfaller, R.1    Kleene, R.2    Neupert, W.3
  • 30
    • 0035193389 scopus 로고    scopus 로고
    • Biochemical characterization of the Arabidopsis biotin synthase reaction. The importance of mitochondria in biotin synthesis
    • Picciocchi A, Douce R, and Alban C (2001) Biochemical characterization of the Arabidopsis biotin synthase reaction. The importance of mitochondria in biotin synthesis. Plant Physiol 127: 1224-1233.
    • (2001) Plant Physiol , vol.127 , pp. 1224-1233
    • Picciocchi, A.1    Douce, R.2    Alban, C.3
  • 31
    • 0025328285 scopus 로고
    • Function of the maize mitochondrial chaperonin hsp60: Specific association between hsp60 and newly synthesized F1-ATPase alpha subunits
    • Prasad TK, Hack E, and Hallberg RL (1990) Function of the maize mitochondrial chaperonin hsp60: specific association between hsp60 and newly synthesized F1-ATPase alpha subunits. Mol Cell Biol 10: 3979-3986.
    • (1990) Mol Cell Biol , vol.10 , pp. 3979-3986
    • Prasad, T.K.1    Hack, E.2    Hallberg, R.L.3
  • 32
    • 0035910001 scopus 로고    scopus 로고
    • Tetrahydrofolate biosynthesis in plants: Molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana
    • Ravanel S, Cherest H, Jabrin S, Grunwald D, Surdin-Kerjan Y, Douce R, and Rebeille F (2001) Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana. Proc Natl Acad Sci USA 98: 15360-15365.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15360-15365
    • Ravanel, S.1    Cherest, H.2    Jabrin, S.3    Grunwald, D.4    Surdin-Kerjan, Y.5    Douce, R.6    Rebeille, F.7
  • 33
    • 0037116605 scopus 로고    scopus 로고
    • Participation of the mitochondrial permeability transition pore in nitric oxide-induced plant cell death
    • Saviani EE, Orsi CH, Oliveira JF, Pinto-Maglio CA, and Salgado I (2002) Participation of the mitochondrial permeability transition pore in nitric oxide-induced plant cell death. FEBS Lett 510: 136-140.
    • (2002) FEBS Lett , vol.510 , pp. 136-140
    • Saviani, E.E.1    Orsi, C.H.2    Oliveira, J.F.3    Pinto-Maglio, C.A.4    Salgado, I.5
  • 34
    • 0035222647 scopus 로고    scopus 로고
    • Blue-native gels to isolate protein complexes from mitochondria
    • Schagger H (2001) Blue-native gels to isolate protein complexes from mitochondria. Methods Cell Biol 65: 231-244.
    • (2001) Methods Cell Biol , vol.65 , pp. 231-244
    • Schagger, H.1
  • 35
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H and von Jagow G (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199: 223-231.
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 36
    • 0029379648 scopus 로고
    • Isolation of a novel Arabidopsis ozone-induced cDNA by differential display
    • Sharma YK and Davis KR (1995) Isolation of a novel Arabidopsis ozone-induced cDNA by differential display. Plant Mol Biol 29: 91-98.
    • (1995) Plant Mol Biol , vol.29 , pp. 91-98
    • Sharma, Y.K.1    Davis, K.R.2
  • 38
    • 0025066552 scopus 로고
    • Pyrroline 5-carboxylate dehydrogenase of the mitochondrial matrix of rat liver. Purification, physical and kinetic characteristics
    • Small WC and Jones ME (1990) Pyrroline 5-carboxylate dehydrogenase of the mitochondrial matrix of rat liver. Purification, physical and kinetic characteristics. J Biol Chem 265: 18668-18672.
    • (1990) J Biol Chem , vol.265 , pp. 18668-18672
    • Small, W.C.1    Jones, M.E.2
  • 41
    • 85039496119 scopus 로고    scopus 로고
    • ExPASy Molecular Biology Server Web site. 1 June
    • Swiss Institute of Bioinformatics. ExPASy Molecular Biology Server Web site. 1 June 2003 〈http://au.expasy.org〉.
    • (2003)
  • 43
    • 0031021278 scopus 로고    scopus 로고
    • The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides
    • Unseld M, Marienfeld JR, Brandt P, and Brennicke A (1997) The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides. Nature Genet 15: 57-61.
    • (1997) Nature Genet , vol.15 , pp. 57-61
    • Unseld, M.1    Marienfeld, J.R.2    Brandt, P.3    Brennicke, A.4
  • 45
    • 0040777075 scopus 로고    scopus 로고
    • Model of a quinary structure between Krebs TCA cycle enzymes: A model for the metabolon
    • Velot C, Mixon MB, Teige M, and Srere PA (1997) Model of a quinary structure between Krebs TCA cycle enzymes: a model for the metabolon. Biochem 36: 14271-14276.
    • (1997) Biochem , vol.36 , pp. 14271-14276
    • Velot, C.1    Mixon, M.B.2    Teige, M.3    Srere, P.A.4


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