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Volumn 390, Issue , 2007, Pages 131-150

In vitro and in vivo methods to study protein import into plant mitochondria

Author keywords

Agrobacterium; Chloroplasts; GFP fusion; Mitochondria; Precursor; Presequence; Protein import; Protoplasts; Targeting peptide; Transient expression

Indexed keywords

GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PROTEIN;

EID: 36549059174     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1385/1-59745-466-4:131     Document Type: Article
Times cited : (5)

References (31)
  • 1
    • 0037447049 scopus 로고    scopus 로고
    • Mechanisms of protein import into mitochondria
    • Truscott, K. N., Brandner, K., and Pfanner, N. (2003) Mechanisms of protein import into mitochondria. Curr. Biol. 13, R326-337.
    • (2003) Curr. Biol , vol.13
    • Truscott, K.N.1    Brandner, K.2    Pfanner, N.3
  • 2
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray, M. W., Burger, G., and Lang, B. F. (1999) Mitochondrial evolution. Scienc, 283, 1476-1481.
    • (1999) Scienc , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 3
    • 0036007390 scopus 로고    scopus 로고
    • Interaction of plant mitochondrial and chloroplast signal peptides with Hsp70 molecular chaperone
    • Zhang, X. P. and Glaser, E. (2002) Interaction of plant mitochondrial and chloroplast signal peptides with Hsp70 molecular chaperone. Trends Plant Sci. 1, 14-21.
    • (2002) Trends Plant Sci , vol.1 , pp. 14-21
    • Zhang, X.P.1    Glaser, E.2
  • 4
    • 33645527869 scopus 로고    scopus 로고
    • Targeting signals and import machinery of plastids and plant mitochondria
    • Danieli, H. and Chase, C, eds, Springer, Dordrecht, The Netherlands, pp
    • Glaser, E. and Soll, J. (2004) Targeting signals and import machinery of plastids and plant mitochondria. In Molecular Biology and Biotechnology of Plant Organelles: Chloroplasts and Mitochondria (Danieli, H. and Chase, C., eds.) Springer, Dordrecht, The Netherlands, pp. 385-418.
    • (2004) Molecular Biology and Biotechnology of Plant Organelles: Chloroplasts and Mitochondria , pp. 385-418
    • Glaser, E.1    Soll, J.2
  • 6
    • 0032738979 scopus 로고    scopus 로고
    • Integration of the mitochondrial processing peptidase into the bel complex of the respiratory chain in plants
    • Glaser, E. and Dessi, P. (1999) Integration of the mitochondrial processing peptidase into the bel complex of the respiratory chain in plants. J. Bioenerg. Biomembr. 31, 259-274.
    • (1999) J. Bioenerg. Biomembr , vol.31 , pp. 259-274
    • Glaser, E.1    Dessi, P.2
  • 7
    • 0036828801 scopus 로고    scopus 로고
    • Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences
    • Stahl, A. Moberg, P., Ytterberg, J., et al. (2002) Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences. J. Biol. Chem. 277, 41931-4939.
    • (2002) J. Biol. Chem , vol.277 , pp. 41931-44939
    • Stahl, A.1    Moberg, P.2    Ytterberg, J.3
  • 8
    • 0344668824 scopus 로고    scopus 로고
    • Characterization of a novel zinc metalloprotease involved in degrading signal peptides in mitochondria and chloroplasts
    • Moberg, P., Ståhl, A., Bhushan, S., et al. (2003) Characterization of a novel zinc metalloprotease involved in degrading signal peptides in mitochondria and chloroplasts. Plant J. 36, 616-628.
    • (2003) Plant J , vol.36 , pp. 616-628
    • Moberg, P.1    Ståhl, A.2    Bhushan, S.3
  • 9
    • 0348133604 scopus 로고    scopus 로고
    • Dual targeting and function of a protease in mitochondria and chloroplasts
    • Bushan, S., Lefebvre, B., Ståhl, A., Boutry, M., and Glaser, E. (2003) Dual targeting and function of a protease in mitochondria and chloroplasts. EMBO Rep. 4, 1073-1078.
    • (2003) EMBO Rep , vol.4 , pp. 1073-1078
    • Bushan, S.1    Lefebvre, B.2    Ståhl, A.3    Boutry, M.4    Glaser, E.5
  • 10
    • 21144447897 scopus 로고    scopus 로고
    • Two novel targeting peptide degrading proteases, PrePs, in mitochondria and chloroplasts, so similar and still different
    • Ståhl, A., Nilsson, S., Lundberg, P., Bhushan, S., et al. (2005) Two novel targeting peptide degrading proteases, PrePs, in mitochondria and chloroplasts, so similar and still different. J. Mol. Biol. 349, 847-860.
    • (2005) J. Mol. Biol , vol.349 , pp. 847-860
    • Ståhl, A.1    Nilsson, S.2    Lundberg, P.3    Bhushan, S.4
  • 12
    • 0029347014 scopus 로고
    • Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco
    • Creissen, G., Reynolds, H., Xue, Y., and Mullineaux, P. (1995) Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco. Plant J. 8, 167-175.
    • (1995) Plant J , vol.8 , pp. 167-175
    • Creissen, G.1    Reynolds, H.2    Xue, Y.3    Mullineaux, P.4
  • 13
    • 0032168849 scopus 로고    scopus 로고
    • Two birds with one stone: Genes that encode products targeted to two or more compartments
    • Small, I., Wintz, H., Akashi, K., and Mireau, H. (1998) Two birds with one stone: genes that encode products targeted to two or more compartments. Plant Mol. Biol. 38, 265-277.
    • (1998) Plant Mol. Biol , vol.38 , pp. 265-277
    • Small, I.1    Wintz, H.2    Akashi, K.3    Mireau, H.4
  • 14
    • 0034330546 scopus 로고    scopus 로고
    • One RNA polymerase serving two genomes
    • Hedtke, B., Borner, T., and Weihe, A. (2000) One RNA polymerase serving two genomes. EMBO Rep. 1, 435-440.
    • (2000) EMBO Rep , vol.1 , pp. 435-440
    • Hedtke, B.1    Borner, T.2    Weihe, A.3
  • 15
    • 0035999898 scopus 로고    scopus 로고
    • A novel in vitro system for simultaneous import of precursor proteins into chloroplast and mitochondria
    • Rudhe, C., Chew, O., Whelan, J., and Glaser, E. (2002) A novel in vitro system for simultaneous import of precursor proteins into chloroplast and mitochondria. Plant J. 30, 213-220.
    • (2002) Plant J , vol.30 , pp. 213-220
    • Rudhe, C.1    Chew, O.2    Whelan, J.3    Glaser, E.4
  • 16
    • 0023224652 scopus 로고
    • Targeting of bacterial chloramphenicol acetyltransferase to mitochondria in transgenic plants
    • Boutry, M., Nagy, F., Poulsen, C., Aoyagi, K., and Chua, N.H. (1987) Targeting of bacterial chloramphenicol acetyltransferase to mitochondria in transgenic plants. Nature 328, 340-342.
    • (1987) Nature , vol.328 , pp. 340-342
    • Boutry, M.1    Nagy, F.2    Poulsen, C.3    Aoyagi, K.4    Chua, N.H.5
  • 17
    • 0024707625 scopus 로고
    • A yeast mitochondrial presequence functions as a signal for targeting to plant mitochondria in-vivo
    • Schmitz, U. K. and Lonsdale, D. M. (1989) A yeast mitochondrial presequence functions as a signal for targeting to plant mitochondria in-vivo. Plant Cell 1, 783-791.
    • (1989) Plant Cell , vol.1 , pp. 783-791
    • Schmitz, U.K.1    Lonsdale, D.M.2
  • 18
    • 0001160047 scopus 로고    scopus 로고
    • Different in vitro and in vivo targeting properties of the transit peptide of a chloroplast envelope inner membrane protein
    • Silva Filho, M. d. C., Wieers, M.-C., Flugge, U.-L, Chaumont, F., and Boutry, M. (1997) Different in vitro and in vivo targeting properties of the transit peptide of a chloroplast envelope inner membrane protein. J. Biol. Chem. 272, 15264-15269.
    • (1997) J. Biol. Chem , vol.272 , pp. 15264-15269
    • Silva Filho, M.D.C.1    Wieers, M.-C.2    Flugge, U.-L.3    Chaumont, F.4    Boutry, M.5
  • 19
    • 0025448659 scopus 로고
    • Sorting of precursor proteins between isolated spinach leaf mitochondria and chloroplasts
    • Whelan, J., Knorpp, C., and Glaser, E. (1990) Sorting of precursor proteins between isolated spinach leaf mitochondria and chloroplasts. Plant Mol. Biol. 14, 977-982.
    • (1990) Plant Mol. Biol , vol.14 , pp. 977-982
    • Whelan, J.1    Knorpp, C.2    Glaser, E.3
  • 21
    • 0032168004 scopus 로고    scopus 로고
    • Protein translocation into and across the chloroplastic envelope membranes
    • Soll, J. and Tien, R. (1998) Protein translocation into and across the chloroplastic envelope membranes. Plant Mol. Biol. 38, 191-207.
    • (1998) Plant Mol. Biol , vol.38 , pp. 191-207
    • Soll, J.1    Tien, R.2
  • 22
    • 0029310448 scopus 로고
    • Peculiar properties of the PsaF photosystem I protein from the green alga Chlamydomonas reinhardtii: Presequence independent import of the PsaF protein into both chloroplasts and mitochondria
    • Hugosson, M., Nurani, G., Glaser, E. and Franzen, L.G. (1995) Peculiar properties of the PsaF photosystem I protein from the green alga Chlamydomonas reinhardtii: presequence independent import of the PsaF protein into both chloroplasts and mitochondria. Plant Mol. Biol. 28, 525-535.
    • (1995) Plant Mol. Biol , vol.28 , pp. 525-535
    • Hugosson, M.1    Nurani, G.2    Glaser, E.3    Franzen, L.G.4
  • 23
    • 0028237677 scopus 로고
    • Preproteins of chloroplast envelope inner membrane contain targeting information for receptor-dependent import into fungal mitochondria
    • Brink, S., Flügge, U. I., Chaumont, F., et al. (1994) Preproteins of chloroplast envelope inner membrane contain targeting information for receptor-dependent import into fungal mitochondria. J. Biol. Chem. 269, 16478-16485.
    • (1994) J. Biol. Chem , vol.269 , pp. 16478-16485
    • Brink, S.1    Flügge, U.I.2    Chaumont, F.3
  • 25
    • 0035850871 scopus 로고    scopus 로고
    • Arabidopsis thaliana ferrochelatase-I and -II are not imported into Arabidopsis mitochondria
    • Lister, R., Chew, O., Lee, M., and Whelan, J. (2001) Arabidopsis thaliana ferrochelatase-I and -II are not imported into Arabidopsis mitochondria. FEBS Lett. 506, 291-295.
    • (2001) FEBS Lett , vol.506 , pp. 291-295
    • Lister, R.1    Chew, O.2    Lee, M.3    Whelan, J.4
  • 26
    • 0037085282 scopus 로고    scopus 로고
    • Isolated plant mitochondria import chloroplast precursor proteins in vitro with the same efficiency as chloroplasts
    • Cleary, S. P., Tan, F.-C, Nakrieko, K.-A., et al. (2002) Isolated plant mitochondria import chloroplast precursor proteins in vitro with the same efficiency as chloroplasts. J. Biol. Chem. 277, 5562-5569.
    • (2002) J. Biol. Chem , vol.277 , pp. 5562-5569
    • Cleary, S.P.1    Tan, F.-C.2    Nakrieko, K.-A.3
  • 27
    • 0034796437 scopus 로고    scopus 로고
    • Hydrophobic residues within the predicted N-terminal amphiphilic alpha-helix of a plant mitochondrial targeting presequence play a major role in in vivo import
    • Duby, G., Oufattole, M., and Boutry, M. (2001) Hydrophobic residues within the predicted N-terminal amphiphilic alpha-helix of a plant mitochondrial targeting presequence play a major role in in vivo import. Plant J. 27, 539-549.
    • (2001) Plant J , vol.27 , pp. 539-549
    • Duby, G.1    Oufattole, M.2    Boutry, M.3
  • 29
    • 0032615881 scopus 로고    scopus 로고
    • Transformation of rice via PEG-mediated DNA uptake into protoplasts
    • Datta, K. and Datta, S.K. (1999) Transformation of rice via PEG-mediated DNA uptake into protoplasts. Meth. Mol. Biol. 111, 335-347.
    • (1999) Meth. Mol. Biol , vol.111 , pp. 335-347
    • Datta, K.1    Datta, S.K.2
  • 30
    • 0346669752 scopus 로고    scopus 로고
    • Characterization of the targeting signal of dual-targeted pea glutathione reductase
    • Chew, O., Rudhe, C., Glaser, E., and Whelan, J. (2003) Characterization of the targeting signal of dual-targeted pea glutathione reductase. Plant Mol. Biol. 53, 341-356.
    • (2003) Plant Mol. Biol , vol.53 , pp. 341-356
    • Chew, O.1    Rudhe, C.2    Glaser, E.3    Whelan, J.4
  • 31
    • 0032077902 scopus 로고    scopus 로고
    • Signs of translational regulation within the transcript leader of a plant plasma membrane H(+)-ATPase gene
    • Lukaszewicz, M., Jerouville, B. and Boutry, M. (1998) Signs of translational regulation within the transcript leader of a plant plasma membrane H(+)-ATPase gene. Plant J. 14, 413-423.
    • (1998) Plant J , vol.14 , pp. 413-423
    • Lukaszewicz, M.1    Jerouville, B.2    Boutry, M.3


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