메뉴 건너뛰기




Volumn 30, Issue 2, 2011, Pages 205-215

Simultaneous isolation of pure and intact chloroplasts and mitochondria from moss as the basis for sub-cellular proteomics

Author keywords

Bryophyte; Chloroplast proteins; Compartment marker; Mitochondrial proteins; Organelles; Physcomitrella

Indexed keywords

ALGAE; BRYOPHYTA; BRYOPHYTES; PHYSCOMITRELLA; PHYSCOMITRELLA PATENS; SPERMATOPHYTA;

EID: 78651446490     PISSN: 07217714     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00299-010-0935-4     Document Type: Article
Times cited : (44)

References (51)
  • 1
    • 2942530586 scopus 로고    scopus 로고
    • Chloroplast proteomics: potentials and challenges
    • Baginski S, Gruissem W (2004) Chloroplast proteomics: potentials and challenges. J Exp Bot 55: 1213-1220.
    • (2004) J Exp Bot , vol.55 , pp. 1213-1220
    • Baginski, S.1    Gruissem, W.2
  • 2
    • 17444429670 scopus 로고    scopus 로고
    • Analysis of shotgun proteomics and RNA profiling data from Arabidopsis thaliana chloroplasts
    • Baginski S, Kleffmann T, von Zychlinski A, Gruissem W (2005) Analysis of shotgun proteomics and RNA profiling data from Arabidopsis thaliana chloroplasts. J Prot Res 4: 637-640.
    • (2005) J Prot Res , vol.4 , pp. 637-640
    • Baginski, S.1    Kleffmann, T.2    von Zychlinski, A.3    Gruissem, W.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0035852227 scopus 로고    scopus 로고
    • The paradox of plastid transit peptides: conservation of function despite divergence in primary structure
    • Bruce BD (2001) The paradox of plastid transit peptides: conservation of function despite divergence in primary structure. Biochim Biophys Acta 1541: 2-21.
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 2-21
    • Bruce, B.D.1
  • 6
    • 33744964949 scopus 로고    scopus 로고
    • Moss systems biology en route: phytohormones in Physcomitrella development
    • Decker EL, Frank W, Sarnighausen E, Reski R (2006) Moss systems biology en route: phytohormones in Physcomitrella development. Plant Biol 8: 397-405.
    • (2006) Plant Biol , vol.8 , pp. 397-405
    • Decker, E.L.1    Frank, W.2    Sarnighausen, E.3    Reski, R.4
  • 7
    • 35448934538 scopus 로고    scopus 로고
    • Free-flow electrophoresis for purification of plant mitochondria by surface charge
    • Eubel H, Lee CP, Kuo J, Meyer EH, Taylor NL, Millar AH (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
  • 8
    • 34548506278 scopus 로고    scopus 로고
    • A mitochondrial protein homologous to the mammalian peripheral-type benzodiazepine receptor is essential for stress adaptation in plants
    • Frank W, Baar KM, Qudeimat E, Woriedh M, Alawady A, Ratnadewi D, Gremillon L, Grimm B, Reski R (2007) A mitochondrial protein homologous to the mammalian peripheral-type benzodiazepine receptor is essential for stress adaptation in plants. Plant J 51: 1004-1018.
    • (2007) Plant J , vol.51 , pp. 1004-1018
    • Frank, W.1    Baar, K.M.2    Qudeimat, E.3    Woriedh, M.4    Alawady, A.5    Ratnadewi, D.6    Gremillon, L.7    Grimm, B.8    Reski, R.9
  • 9
    • 0033179331 scopus 로고    scopus 로고
    • The use of chloromethyl-X-rosamine (Mitotracker red) to measure loss of mitochondrial membrane potential in apoptotic cells is incompatible with cell fixation
    • Gilmore K, Wilson M (1999) The use of chloromethyl-X-rosamine (Mitotracker red) to measure loss of mitochondrial membrane potential in apoptotic cells is incompatible with cell fixation. Cytometry 36: 355-358.
    • (1999) Cytometry , vol.36 , pp. 355-358
    • Gilmore, K.1    Wilson, M.2
  • 10
    • 33747046042 scopus 로고    scopus 로고
    • The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short- and long-term exposure to low temperature
    • Goulas E, Schubert M, Kieselbach T, Kleczkowski LA, Gardestrom P, Schroder W, Hurry V (2006) The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short- and long-term exposure to low temperature. Plant J 47: 720-734.
    • (2006) Plant J , vol.47 , pp. 720-734
    • Goulas, E.1    Schubert, M.2    Kieselbach, T.3    Kleczkowski, L.A.4    Gardestrom, P.5    Schroder, W.6    Hurry, V.7
  • 11
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray MW, Burger G, Lang BF (1999) Mitochondrial evolution. Science 283: 1476-1481.
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 13
    • 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 JL, Tonti-Filippini JS, Gout AM, Day DA, Whelan J, Millar AH (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
  • 14
    • 2342518184 scopus 로고    scopus 로고
    • An efficient protocol for the identification of protein phosphorylation in a seedless plant, sensitive enough to detect members of signalling cascades
    • Heintz D, Wurtz V, High AA, van Dorsselaer A, Reski R, Sarnighausen E (2004) An efficient protocol for the identification of protein phosphorylation in a seedless plant, sensitive enough to detect members of signalling cascades. Electrophoresis 25: 1149-1159.
    • (2004) Electrophoresis , vol.25 , pp. 1149-1159
    • Heintz, D.1    Wurtz, V.2    High, A.A.3    van Dorsselaer, A.4    Reski, R.5    Sarnighausen, E.6
  • 16
    • 60249086737 scopus 로고    scopus 로고
    • Experimental analysis of the rice mitochondrial proteome, its biogenesis, and heterogeneity
    • Huang S, Taylor NL, Narsai R, Eubel H, Whelan J, Millar AH (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
  • 17
    • 25844490674 scopus 로고    scopus 로고
    • Unique translation initiation at the second AUG codon determines mitochondrial localization of the phage-type RNA polymerases in the moss Physcomitrella patens
    • Kabeya Y, Sato N (2005) Unique translation initiation at the second AUG codon determines mitochondrial localization of the phage-type RNA polymerases in the moss Physcomitrella patens. Plant Physiol 138: 369-382.
    • (2005) Plant Physiol , vol.138 , pp. 369-382
    • Kabeya, Y.1    Sato, N.2
  • 18
    • 0030910725 scopus 로고    scopus 로고
    • Cytokinin affects nuclear- and plastome-encoded energy-converting plastid enzymes
    • Kasten B, Buck F, Nuske J, Reski R (1997) Cytokinin affects nuclear- and plastome-encoded energy-converting plastid enzymes. Planta 201: 261-272.
    • (1997) Planta , vol.201 , pp. 261-272
    • Kasten, B.1    Buck, F.2    Nuske, J.3    Reski, R.4
  • 22
    • 77649179118 scopus 로고    scopus 로고
    • Isolating intact chloroplasts from small Arabidopsis samples for proteomic studies
    • Kley J, Heil M, Muck A, Svatos A, Boland W (2010) Isolating intact chloroplasts from small Arabidopsis samples for proteomic studies. Anal Biochem 398: 198-202.
    • (2010) Anal Biochem , vol.398 , pp. 198-202
    • Kley, J.1    Heil, M.2    Muck, A.3    Svatos, A.4    Boland, W.5
  • 23
    • 34547959775 scopus 로고    scopus 로고
    • The putative moss 3′phosphoadenosine 5′phosphosulfate reductase is a novel form of adenosine 5′phosphosulfate reductase without an iron sulfur cluster
    • Kopriva S, Fritzemeier K, Wiedemann G, Reski R (2007) The putative moss 3′phosphoadenosine 5′phosphosulfate reductase is a novel form of adenosine 5′phosphosulfate reductase without an iron sulfur cluster. J Biol Chem 282: 22930-22938.
    • (2007) J Biol Chem , vol.282 , pp. 22930-22938
    • Kopriva, S.1    Fritzemeier, K.2    Wiedemann, G.3    Reski, R.4
  • 24
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft V, Eubel H, Jansch L, Werhahn W, 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
  • 25
    • 47849117424 scopus 로고    scopus 로고
    • Heterogeneity of the mitochondrial proteome for photosynthetic and non-photosynthetic Arabidopsis metabolism
    • Lee CP, Eubel H, O'Toole N, Millar AH (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
  • 27
    • 0005243302 scopus 로고
    • Isolation of nuclear, chloroplast and mitochondrial DNA from the moss Physcomitrella patens
    • Marienfeld JR, Reski R, Friese C, Abel WO (1989) Isolation of nuclear, chloroplast and mitochondrial DNA from the moss Physcomitrella patens. Plant Sci 61: 235-244.
    • (1989) Plant Sci , vol.61 , pp. 235-244
    • Marienfeld, J.R.1    Reski, R.2    Friese, C.3    Abel, W.O.4
  • 28
    • 0001458708 scopus 로고
    • Simplified procedure for the isolation of intact chloroplasts from Chlamydomonas reinhardtii
    • Mason CB, Matthews S, Bricker TM, Moroney JV (1991) Simplified procedure for the isolation of intact chloroplasts from Chlamydomonas reinhardtii. Plant Physiol 97: 1576-1580.
    • (1991) Plant Physiol , vol.97 , pp. 1576-1580
    • Mason, C.B.1    Matthews, S.2    Bricker, T.M.3    Moroney, J.V.4
  • 29
    • 0032052217 scopus 로고    scopus 로고
    • Cytofluorometric detection of mitochondrial alterations in early CD95/Fas/APO-1-triggered apoptosis of Jurkat T lymphoma cells. Comparison of seven mitochondrion-specific fluorochromes
    • Metivier D, Dallaporta B, Zamzami N, Larochette N, Susin SA, Marzo I, Kroemer G (1998) Cytofluorometric detection of mitochondrial alterations in early CD95/Fas/APO-1-triggered apoptosis of Jurkat T lymphoma cells. Comparison of seven mitochondrion-specific fluorochromes. Immunol Lett 61: 157-163.
    • (1998) Immunol Lett , vol.61 , pp. 157-163
    • Metivier, D.1    Dallaporta, B.2    Zamzami, N.3    Larochette, N.4    Susin, S.A.5    Marzo, I.6    Kroemer, G.7
  • 30
    • 0035231382 scopus 로고    scopus 로고
    • Isolation and subfractionation of mitochondria from plants
    • Millar AH, Liddell A, Leaver CJ (2001a) Isolation and subfractionation of mitochondria from plants. Methods Cell Biol 65: 53-74.
    • (2001) Methods Cell Biol , vol.65 , pp. 53-74
    • Millar, A.H.1    Liddell, A.2    Leaver, C.J.3
  • 36
    • 0031930234 scopus 로고    scopus 로고
    • Development, genetics and molecular biology of mosses
    • Reski R (1998) Development, genetics and molecular biology of mosses. Bot Acta 111: 1-15.
    • (1998) Bot Acta , vol.111 , pp. 1-15
    • Reski, R.1
  • 37
    • 70349439088 scopus 로고    scopus 로고
    • Challenges to our current view on chloroplasts
    • Reski R (2009) Challenges to our current view on chloroplasts. Biol Chem 390: 731-738.
    • (2009) Biol Chem , vol.390 , pp. 731-738
    • Reski, R.1
  • 38
    • 0001693751 scopus 로고
    • Induction of budding on chloronemata and caulonemata of the moss, Physcomitrella patens, using isopentenyladenine
    • Reski R, Abel WO (1985) Induction of budding on chloronemata and caulonemata of the moss, Physcomitrella patens, using isopentenyladenine. Planta 165: 354-358.
    • (1985) Planta , vol.165 , pp. 354-358
    • Reski, R.1    Abel, W.O.2
  • 39
    • 34249792100 scopus 로고    scopus 로고
    • PlanTAPDB, a phylogeny-based resource of plant transcription-associated proteins
    • Richardt S, Lang D, Reski R, Frank W, Rensing SA (2007) PlanTAPDB, a phylogeny-based resource of plant transcription-associated proteins. Plant Physiol 143: 1452-1466.
    • (2007) Plant Physiol , vol.143 , pp. 1452-1466
    • Richardt, S.1    Lang, D.2    Reski, R.3    Frank, W.4    Rensing, S.A.5
  • 40
    • 72149091719 scopus 로고    scopus 로고
    • Microarray analysis of the moss Physcomitrella patens reveals evolutionarily conserved transcriptional regulation of salt stress and abscisic acid signalling
    • Richardt S, Timmerhaus G, Lang D, Qudeimat E, Correa LG, Reski R, Rensing SA, Frank W (2010) Microarray analysis of the moss Physcomitrella patens reveals evolutionarily conserved transcriptional regulation of salt stress and abscisic acid signalling. Plant Mol Biol 72: 27-45.
    • (2010) Plant Mol Biol , vol.72 , pp. 27-45
    • Richardt, S.1    Timmerhaus, G.2    Lang, D.3    Qudeimat, E.4    Correa, L.G.5    Reski, R.6    Rensing, S.A.7    Frank, W.8
  • 41
    • 0037094426 scopus 로고    scopus 로고
    • Two RpoT genes of Physcomitrella patens encode phage-type RNA polymerases with dual targeting to mitochondria and plastids
    • Richter U, Kiessling J, Hedtke B, Decker E, Reski R, Börner T, Weihe A (2002) Two RpoT genes of Physcomitrella patens encode phage-type RNA polymerases with dual targeting to mitochondria and plastids. Gene 290: 95-105.
    • (2002) Gene , vol.290 , pp. 95-105
    • Richter, U.1    Kiessling, J.2    Hedtke, B.3    Decker, E.4    Reski, R.5    Börner, T.6    Weihe, A.7
  • 43
    • 84934441050 scopus 로고    scopus 로고
    • Purification and proteomic analysis of chloroplasts and their sub-organellar compartments
    • Salvi D, Rolland N, Joyard J, Ferro M (2008a) Purification and proteomic analysis of chloroplasts and their sub-organellar compartments. Methods Mol Biol 432: 19-36.
    • (2008) Methods Mol Biol , vol.432 , pp. 19-36
    • Salvi, D.1    Rolland, N.2    Joyard, J.3    Ferro, M.4
  • 44
    • 84934443244 scopus 로고    scopus 로고
    • Assessment of organelle purity using antibodies and specific assays: the example of the chloroplast envelope
    • Salvi D, Rolland N, Joyard J, Ferro M (2008b) Assessment of organelle purity using antibodies and specific assays: the example of the chloroplast envelope. Methods Mol Biol 432: 345-356.
    • (2008) Methods Mol Biol , vol.432 , pp. 345-356
    • Salvi, D.1    Rolland, N.2    Joyard, J.3    Ferro, M.4
  • 45
    • 57749098549 scopus 로고    scopus 로고
    • The mitochondrial cycle of Arabidopsis shoot apical meristem and leaf primordium meristematic cells is defined by a perinuclear tentaculate/cage-like mitochondrion
    • Segui-Simarro JM, Coronado MJ, Staehelin LA (2008) The mitochondrial cycle of Arabidopsis shoot apical meristem and leaf primordium meristematic cells is defined by a perinuclear tentaculate/cage-like mitochondrion. Plant Physiol 148: 1380-1393.
    • (2008) Plant Physiol , vol.148 , pp. 1380-1393
    • Segui-Simarro, J.M.1    Coronado, M.J.2    Staehelin, L.A.3
  • 46
    • 77954746076 scopus 로고    scopus 로고
    • The chloroplast protein import machinery: a review
    • Strittmatter P, Soll J, Bolter B (2010) The chloroplast protein import machinery: a review. Methods Mol Biol 619: 307-321.
    • (2010) Methods Mol Biol , vol.619 , pp. 307-321
    • Strittmatter, P.1    Soll, J.2    Bolter, B.3
  • 48
    • 40949146548 scopus 로고    scopus 로고
    • Isolation of intact, functional mitochondria from the model plant Arabidopsis thaliana
    • Sweetlove LJ, Taylor NL, Leaver CJ (2007) Isolation of intact, functional mitochondria from the model plant Arabidopsis thaliana. Methods Mol Biol 372: 125-136.
    • (2007) Methods Mol Biol , vol.372 , pp. 125-136
    • Sweetlove, L.J.1    Taylor, N.L.2    Leaver, C.J.3
  • 49
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D, Flügge UI (1984) A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal Biochem 138: 141-143.
    • (1984) Anal Biochem , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 50
    • 77952957983 scopus 로고    scopus 로고
    • Targeted knock-out of a gene encoding sulfite reductase in the moss Physcomitrella patens affects gametophytic and sporophytic development
    • Wiedemann G, Hermsen C, Melzer M, Büttner-Mainik A, Renneberg H, Reski R, Kopriva S (2010) Targeted knock-out of a gene encoding sulfite reductase in the moss Physcomitrella patens affects gametophytic and sporophytic development. FEBS Lett 584: 2271-2278.
    • (2010) FEBS Lett , vol.584 , pp. 2271-2278
    • Wiedemann, G.1    Hermsen, C.2    Melzer, M.3    Büttner-Mainik, A.4    Renneberg, H.5    Reski, R.6    Kopriva, S.7
  • 51
    • 34548297894 scopus 로고    scopus 로고
    • The PsbP protein is required for photosystem II complex assembly/stability and photoautotrophy in Arabidopsis thaliana
    • Yi X, Hargett SR, Liu H, Frankel LK, Bricker TM (2007) The PsbP protein is required for photosystem II complex assembly/stability and photoautotrophy in Arabidopsis thaliana. J Biol Chem 282: 24833-24841.
    • (2007) J Biol Chem , vol.282 , pp. 24833-24841
    • Yi, X.1    Hargett, S.R.2    Liu, H.3    Frankel, L.K.4    Bricker, T.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.