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Volumn 209, Issue 3, 1999, Pages 267-274

The protein-import apparatus of plant mitochondria

Author keywords

Chaperone; Import apparatus; Plant mitochondria; Preprotein translocase; Processing peptidase; Protein; Protein transport

Indexed keywords

CELL TRANSPORT; CELLULAR DISTRIBUTION; MITOCHONDRION; PROTEIN FUNCTION;

EID: 0033198449     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050632     Document Type: Review
Times cited : (45)

References (79)
  • 2
    • 0029070886 scopus 로고
    • The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system
    • Berthold J, Bauer MF, Schneider HC, Klaus C, Dietmeier K, Neupert W, Brunner M (1995) The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system. Cell 81: 1085-1093
    • (1995) Cell , vol.81 , pp. 1085-1093
    • Berthold, J.1    Bauer, M.F.2    Schneider, H.C.3    Klaus, C.4    Dietmeier, K.5    Neupert, W.6    Brunner, M.7
  • 3
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria
    • Bogsch EG, Sargent F, Stanley NR, Berks BC, Robinson C, Palmer T (1998) An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J Biol Chem 273: 18003-18006
    • (1998) J Biol Chem , vol.273 , pp. 18003-18006
    • Bogsch, E.G.1    Sargent, F.2    Stanley, N.R.3    Berks, B.C.4    Robinson, C.5    Palmer, T.6
  • 4
    • 0030569015 scopus 로고    scopus 로고
    • The preprotein translocase of the inner mitochondrial membrane: Evolutionary conservation of targeting and assembly of Tim17
    • Bömer U, Rassow J, Zufall N, Pfanner N, Meijer M, Maarse AC (1996) The preprotein translocase of the inner mitochondrial membrane: evolutionary conservation of targeting and assembly of Tim17. J Mol Biol 262: 389-395
    • (1996) J Mol Biol , vol.262 , pp. 389-395
    • Bömer, U.1    Rassow, J.2    Zufall, N.3    Pfanner, N.4    Meijer, M.5    Maarse, A.C.6
  • 5
    • 0029066902 scopus 로고
    • 2 complex evolutionary relics of a processing peptidase?
    • 2 complex evolutionary relics of a processing peptidase? Trends Biochem Sci 20: 171-175
    • (1995) Trends Biochem Sci , vol.20 , pp. 171-175
    • Braun, H.P.1    Schmitz, U.K.2
  • 6
    • 0030728696 scopus 로고    scopus 로고
    • Molecules in focus: The cytochrome c reduclase/mitochondrial processing peptidase complex
    • Braun HP, Schmitz UK (1997) Molecules in focus: the cytochrome c reduclase/mitochondrial processing peptidase complex. Int J Biochem Cell Biol 29: 1043-1045
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 1043-1045
    • Braun, H.P.1    Schmitz, U.K.2
  • 7
    • 0026709336 scopus 로고
    • The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain
    • Braun HP, Emmermann M, Kruft V, Schmitz UK (1992a) The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J 11: 3219-3227
    • (1992) EMBO J , vol.11 , pp. 3219-3227
    • Braun, H.P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 8
    • 0026610063 scopus 로고
    • 1 from potato: A protein with a presequence for targeting to the mitochondrial intermembrane space
    • 1 from potato: a protein with a presequence for targeting to the mitochondrial intermembrane space. Mol Gen Genet 231: 217-225
    • (1992) Mol Gen Genet , vol.231 , pp. 217-225
    • Braun, H.P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 10
    • 0028237677 scopus 로고
    • Preproteins of chloroplast envelope inner membrane contain targeting information for receptor-dependent import into fungal mitochondria
    • Brink S, Flügge UI, Chaumont F, Boutry M, Emmermann M, Schmitz UK, Becker K, Pfanner N (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    Boutry, M.4    Emmermann, M.5    Schmitz, U.K.6    Becker, K.7    Pfanner, N.8
  • 11
    • 0032557434 scopus 로고    scopus 로고
    • New insights into the co-evolution of cytochrome c reductase and the mitochondrial processing peptidase
    • Brumme S, Kruft V, Schmitz UK, Braun HP (1998) New insights into the co-evolution of cytochrome c reductase and the mitochondrial processing peptidase. J Biol Chem 273: 13143-13149
    • (1998) J Biol Chem , vol.273 , pp. 13143-13149
    • Brumme, S.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 12
    • 0028197674 scopus 로고
    • Identification of chaperonin-10 homologue in plant mitochondria
    • Burt WJE, Leaver CJ (1994) Identification of chaperonin-10 homologue in plant mitochondria. FEBS Lett. 339: 139-141
    • (1994) FEBS Lett. , vol.339 , pp. 139-141
    • Burt, W.J.E.1    Leaver, C.J.2
  • 13
    • 0029079118 scopus 로고
    • A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the delta pH-depentent thylakoidal protein translocate
    • Chaddock AM, Mant A, Karnauchow I, Brink S, Herrmann RG, Klösgen RB, Robinson C (1995) A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-depentent thylakoidal protein translocate. EMBO J. 14: 2715-2722
    • (1995) EMBO J. , vol.14 , pp. 2715-2722
    • Chaddock, A.M.1    Mant, A.2    Karnauchow, I.3    Brink, S.4    Herrmann, R.G.5    Klösgen, R.B.6    Robinson, C.7
  • 14
    • 0004978030 scopus 로고
    • Protein import into plant mitochondria
    • Levings III, CS, Vasil I.K. (eds) Kluwer, Dordrecht
    • Chaumont F, Boutry M (1995) Protein import into plant mitochondria. In: Levings III, CS, Vasil I.K. (eds) The molecular biology of plant mitochondria. Kluwer, Dordrecht, pp 207-235
    • (1995) The Molecular Biology of Plant Mitochondria , pp. 207-235
    • Chaumont, F.1    Boutry, M.2
  • 15
    • 0025075437 scopus 로고
    • Protein transport into mitochondria is conserved between plant and yeast species
    • Chaumont F, O'Riordan V, Boutry M (1990) Protein transport into mitochondria is conserved between plant and yeast species. J Biol Chem 265: 16856-16862
    • (1990) J Biol Chem , vol.265 , pp. 16856-16862
    • Chaumont, F.1    O'Riordan, V.2    Boutry, M.3
  • 16
    • 0030786269 scopus 로고    scopus 로고
    • A single protein for ferrochelatase-I from Arabidopsis is imported in vitro into both chloroplasts and mitochondria
    • Chow KS, Singh DP, Roper JM, Smith AG (1997) A single protein for ferrochelatase-I from Arabidopsis is imported in vitro into both chloroplasts and mitochondria. J Biol Chem 272: 27565-27571
    • (1997) J Biol Chem , vol.272 , pp. 27565-27571
    • Chow, K.S.1    Singh, D.P.2    Roper, J.M.3    Smith, A.G.4
  • 17
    • 0028438050 scopus 로고
    • Isolation of a full-length cDNA encoding Brassica napus mitochondrial chaperonin-60
    • Cole KP, Blakeley SD, Dennis DT (1994) Isolation of a full-length cDNA encoding Brassica napus mitochondrial chaperonin-60. Plant Physiol. 105: 451
    • (1994) Plant Physiol. , vol.105 , pp. 451
    • Cole, K.P.1    Blakeley, S.D.2    Dennis, D.T.3
  • 18
    • 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, 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
  • 20
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies RJ, Koch BD, Werner-Washburne M, Craig EA, Schekman R (1988) A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332: 800-805
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 21
    • 0027130557 scopus 로고
    • The cytochrome c reductase integrated processing peptidase from potato mitochondria belongs to a new class of metalloendoproteases
    • Emmermann M, Schmitz UK (1993) The cytochrome c reductase integrated processing peptidase from potato mitochondria belongs to a new class of metalloendoproteases. Plant Physiol. 103: 615-620
    • (1993) Plant Physiol. , vol.103 , pp. 615-620
    • Emmermann, M.1    Schmitz, U.K.2
  • 22
    • 0029284709 scopus 로고
    • Two cDNA isoforms of the β-subunit of the general mitochondrial processing peptidase from potato
    • Emmermann M, Schmitz UK (1995) Two cDNA isoforms of the β-subunit of the general mitochondrial processing peptidase from potato. Plant Physiol. 107: 1467-1468
    • (1995) Plant Physiol. , vol.107 , pp. 1467-1468
    • Emmermann, M.1    Schmitz, U.K.2
  • 23
    • 0027225845 scopus 로고
    • Characterization of the bifunctional cytochrome c reductase/processing peptidase complex from potato mitochondria
    • Emmermann M, Braun HP, Arretz M, Schmitz UK (1993) Characterization of the bifunctional cytochrome c reductase/processing peptidase complex from potato mitochondria. J. Biol. Chem. 268: 18936-18942
    • (1993) J. Biol. Chem. , vol.268 , pp. 18936-18942
    • Emmermann, M.1    Braun, H.P.2    Arretz, M.3    Schmitz, U.K.4
  • 24
    • 0028072873 scopus 로고
    • The mitochondrial processing peptidase from potato: A self-processing enzyme encoded by two differentially expressed genes
    • Emmermann M, Braun HP, Schmitz UK (1994a) The mitochondrial processing peptidase from potato: A self-processing enzyme encoded by two differentially expressed genes. Mol. Gen. Genet. 245: 237-245
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 237-245
    • Emmermann, M.1    Braun, H.P.2    Schmitz, U.K.3
  • 26
    • 0000749103 scopus 로고
    • 1 complex of the respiratory chain
    • Brennicke A, Kück U (eds) VCH Verlagsgesellschaft, Weinheim
    • 1 complex of the respiratory chain. In: Brennicke A, Kück U (eds) Plant mitochondria. VCH Verlagsgesellschaft, Weinheim pp 299-306
    • (1993) Plant Mitochondria , pp. 299-306
    • Eriksson, A.C.1    Sjöling, S.2    Glaser, E.3
  • 27
    • 0028075242 scopus 로고
    • The ubiquinol cytochrome c oxidoreductase complex of spinach leaf mitochondria is involved in both respiration and protein processing
    • Eriksson AC, Sjöling S, Glaser E (1994) The ubiquinol cytochrome c oxidoreductase complex of spinach leaf mitochondria is involved in both respiration and protein processing. Biochim. Biophys. Acta 1186: 221-231
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 221-231
    • Eriksson, A.C.1    Sjöling, S.2    Glaser, E.3
  • 30
    • 10244239321 scopus 로고    scopus 로고
    • Life with 6000 genes
    • Goffeau A et al. (1996) Life with 6000 genes. Science 274: 546-567
    • (1996) Science , vol.274 , pp. 546-567
    • Goffeau, A.1
  • 31
    • 0032051742 scopus 로고    scopus 로고
    • The organization and evolution of the spinach stress 70 molecular chaperone gene family
    • Guy CL, Li QB (1998) The organization and evolution of the spinach stress 70 molecular chaperone gene family. Plant Cell 10: 539-556
    • (1998) Plant Cell , vol.10 , pp. 539-556
    • Guy, C.L.1    Li, Q.B.2
  • 32
    • 0031466020 scopus 로고    scopus 로고
    • Functional complementation of an oxal yeast mutation identifies an Arabidopsis thaliana cDNA involved in the assembly of respiratory complexes
    • Hamel P, Sakamoto W, Wintz H, Dujardin G (1997) Functional complementation of an oxal yeast mutation identifies an Arabidopsis thaliana cDNA involved in the assembly of respiratory complexes. Plant J. 12: 1319-1327
    • (1997) Plant J. , vol.12 , pp. 1319-1327
    • Hamel, P.1    Sakamoto, W.2    Wintz, H.3    Dujardin, G.4
  • 33
    • 0026648354 scopus 로고
    • Heat shock proteins of barley mitochondria and chloroplasts. Identification of organellar hsp10 and 12: Putative chaperonin 10 homologues
    • Hartman DJ, Dougan D, Hoogenraad NJ, Hoj PB (1992) Heat shock proteins of barley mitochondria and chloroplasts. Identification of organellar hsp10 and 12: putative chaperonin 10 homologues. FEBS Lett. 305: 147-150
    • (1992) FEBS Lett. , vol.305 , pp. 147-150
    • Hartman, D.J.1    Dougan, D.2    Hoogenraad, N.J.3    Hoj, P.B.4
  • 34
    • 0030160495 scopus 로고    scopus 로고
    • A receptor for protein import into potato mitochondria
    • Heins L, Schmitz UK (1996) A receptor for protein import into potato mitochondria. Plant J. 9: 829-839
    • (1996) Plant J. , vol.9 , pp. 829-839
    • Heins, L.1    Schmitz, U.K.2
  • 35
    • 0032004983 scopus 로고    scopus 로고
    • The protein translocation apparatus of chloroplast envelopes
    • Heins L, Collinson I, Soll J (1998) The protein translocation apparatus of chloroplast envelopes. Trends Plant Sci 3: 56-61
    • (1998) Trends Plant Sci , vol.3 , pp. 56-61
    • Heins, L.1    Collinson, I.2    Soll, J.3
  • 36
    • 0030656514 scopus 로고    scopus 로고
    • Oxalp mediates the export of the N- and C-termini of pCoxII from the mitochondrial matrix to the intermembrane space
    • Hell K, Herrmann JM, Pratje E, Neupert W, Stuart RA (1997) Oxalp mediates the export of the N- and C-termini of pCoxII from the mitochondrial matrix to the intermembrane space. FEBS Lett. 418: 6367-6370
    • (1997) FEBS Lett. , vol.418 , pp. 6367-6370
    • Hell, K.1    Herrmann, J.M.2    Pratje, E.3    Neupert, W.4    Stuart, R.A.5
  • 38
    • 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 UK, 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
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 39
    • 0032479295 scopus 로고    scopus 로고
    • Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants
    • Jänsch L, Kruft V, Schmitz UK, Braun HP (1998a) Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants. J Biol Chem 273: 17251-17257
    • (1998) J Biol Chem , vol.273 , pp. 17251-17257
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 40
    • 0037610716 scopus 로고    scopus 로고
    • The TOM complex from plant mitochondria
    • Moller IM, Gardeström P, Glimelius K, Glaser E (eds) Blackhuys Publishers, Leiden
    • Jänsch L, Heins L, Schmitz UK, Braun HP (1998b) The TOM complex from plant mitochondria. In: Moller IM, Gardeström P, Glimelius K, Glaser E (eds) Plant mitochondria: From gene to function. Blackhuys Publishers, Leiden, pp 225-230
    • (1998) Plant Mitochondria: From Gene to Function , pp. 225-230
    • Jänsch, L.1    Heins, L.2    Schmitz, U.K.3    Braun, H.P.4
  • 41
    • 0026638856 scopus 로고
    • Rat liver mitochondrial intermediate peptidase (MIP): Purification and initial characterization
    • Kalousek F, Isaya G, Rosenberg LE (1992) Rat liver mitochondrial intermediate peptidase (MIP): purification and initial characterization. EMBO J. 11: 2803-2809
    • (1992) EMBO J. , vol.11 , pp. 2803-2809
    • Kalousek, F.1    Isaya, G.2    Rosenberg, L.E.3
  • 42
    • 0027222799 scopus 로고
    • Uniform nomenclature for the mitochondrial peptidases cleaving precursors of mitochondrial proteins
    • Kalousek F, Neupert W, Omura T, Schatz G, Schmitz UK (1993) Uniform nomenclature for the mitochondrial peptidases cleaving precursors of mitochondrial proteins. Trends Biol. Sci. 18: 249
    • (1993) Trends Biol. Sci. , vol.18 , pp. 249
    • Kalousek, F.1    Neupert, W.2    Omura, T.3    Schatz, G.4    Schmitz, U.K.5
  • 43
    • 0031408095 scopus 로고    scopus 로고
    • The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane
    • Kerscher O, Holder J, Srinivasan M, Leung RS, Jensen RE (1997) The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane. J. Cell Biol. 139: 1663-1675
    • (1997) J. Cell Biol. , vol.139 , pp. 1663-1675
    • Kerscher, O.1    Holder, J.2    Srinivasan, M.3    Leung, R.S.4    Jensen, R.E.5
  • 44
    • 0025606107 scopus 로고
    • Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins
    • Kiebler M, Pfaller R, Söllner S, Griffiths G, Horstmann H, Pfanner N, Neupert W (1990) Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins. Nature 348: 610-616
    • (1990) Nature , vol.348 , pp. 610-616
    • Kiebler, M.1    Pfaller, R.2    Söllner, S.3    Griffiths, G.4    Horstmann, H.5    Pfanner, N.6    Neupert, W.7
  • 47
    • 0030453894 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA encoding mitochondrial chaperonin-10 from Arabidopsis thaliana by functional complementation of an Escherichia coli groES mutant
    • Koumoto Y, Tsugeki R, Shimada T, Mori H, Kondo M, Hara-Nishimura I, Nishimura M (1996) Isolation and characterization of a cDNA encoding mitochondrial chaperonin-10 from Arabidopsis thaliana by functional complementation of an Escherichia coli groES mutant. Plant J. 10: 1119-1125
    • (1996) Plant J. , vol.10 , pp. 1119-1125
    • Koumoto, Y.1    Tsugeki, R.2    Shimada, T.3    Mori, H.4    Kondo, M.5    Hara-Nishimura, I.6    Nishimura, M.7
  • 48
    • 0030175178 scopus 로고    scopus 로고
    • AtJ1, a mitochondrial homologue of the Escherichia coli DnaJ protein
    • Kroczynska B, Zhou R, Wood C, Miernyk JA (1996) AtJ1, a mitochondrial homologue of the Escherichia coli DnaJ protein. Plant Mol. Biol. 31: 619-629
    • (1996) Plant Mol. Biol. , vol.31 , pp. 619-629
    • Kroczynska, B.1    Zhou, R.2    Wood, C.3    Miernyk, J.A.4
  • 49
    • 0028965679 scopus 로고    scopus 로고
    • Genetic and biochemical dissection of the mitochondrial protein-import machinery
    • Kübrich M, Dietmeier K, Pfanner N (1996) Genetic and biochemical dissection of the mitochondrial protein-import machinery. Curr. Genet. 27: 393-403
    • (1996) Curr. Genet. , vol.27 , pp. 393-403
    • Kübrich, M.1    Dietmeier, K.2    Pfanner, N.3
  • 50
    • 0032167639 scopus 로고    scopus 로고
    • A single gene of chloroplast origin codes for mitochondrial and chloroplastic methionyl-tRNA synthetase in Arabidopsis thaliana
    • Menand B, Maréchal-Drouard L, Sakamoto W, Dietrich A, Wintz H (1998) A single gene of chloroplast origin codes for mitochondrial and chloroplastic methionyl-tRNA synthetase in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 95: 11014-11019
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11014-11019
    • Menand, B.1    Maréchal-Drouard, L.2    Sakamoto, W.3    Dietrich, A.4    Wintz, H.5
  • 53
    • 0032572109 scopus 로고    scopus 로고
    • Mitochondrial protein import in animais
    • Mori M, Terada K (1998) Mitochondrial protein import in animais. Biochim. Biophys. Acta 1403: 12-27
    • (1998) Biochim. Biophys. Acta , vol.1403 , pp. 12-27
    • Mori, M.1    Terada, K.2
  • 55
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W (1997) Protein import into mitochondria. Annu. Rev. Biochem. 66: 863-917
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 56
    • 0027752461 scopus 로고
    • A mitochondrial protease with two catalytic subunits of nonoverlapping specificities
    • Nunnari J, Fox TD, Walter P (1993) A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 262: 1997-2004
    • (1993) Science , vol.262 , pp. 1997-2004
    • Nunnari, J.1    Fox, T.D.2    Walter, P.3
  • 57
    • 0033103034 scopus 로고    scopus 로고
    • Molecular characterization of a plant mitochondrial chaperone GrpE
    • Padidam M, Reddy VS, Beachy RN, Fauquet CM (1999) Molecular characterization of a plant mitochondrial chaperone GrpE. Plant Mol Biol 39: 871-881
    • (1999) Plant Mol Biol , vol.39 , pp. 871-881
    • Padidam, M.1    Reddy, V.S.2    Beachy, R.N.3    Fauquet, C.M.4
  • 58
    • 0028945063 scopus 로고
    • Identification of a 42-kDa plant mitochondrial outer membrane protein, TOM42, involved in the import of precursor proteins into plant mitochondria
    • Perryman RA, Mooney B, Harmey MA (1995) Identification of a 42-kDa plant mitochondrial outer membrane protein, TOM42, involved in the import of precursor proteins into plant mitochondria. Arch Biochem Biophy 316: 659-664
    • (1995) Arch Biochem Biophy , vol.316 , pp. 659-664
    • Perryman, R.A.1    Mooney, B.2    Harmey, M.A.3
  • 61
    • 0039333871 scopus 로고
    • Identification and metabolic characterization of the Zea mays mitochondrial homolog of the Escherichia coli groEL protein
    • Prasad TK, Hallberg RL (1989) Identification and metabolic characterization of the Zea mays mitochondrial homolog of the Escherichia coli groEL protein. Plant Mol. Biol. 12: 609-618
    • (1989) Plant Mol. Biol. , vol.12 , pp. 609-618
    • Prasad, T.K.1    Hallberg, R.L.2
  • 62
    • 0026832009 scopus 로고
    • cDNA clones encoding Arabidopsis thaliana und Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock
    • Prasad TK, Stewart CR (1992) cDNA clones encoding Arabidopsis thaliana und Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock. Plant Mol. Biol. 18: 873-885
    • (1992) Plant Mol. Biol. , vol.18 , pp. 873-885
    • Prasad, T.K.1    Stewart, C.R.2
  • 63
    • 0024707625 scopus 로고
    • A yeast mitochondrial presequence functions as a signal for targeting to plant mitochondria in vivo
    • Schmitz UK, Lonsdale DM (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
  • 64
    • 0026098773 scopus 로고
    • Inner membrane protease 1, an enzyme mediating intramitochondrial protein sorting in yeast
    • Schneider A, Behrens M, Scherer P, Pratje E, Michaelis G, Schatz G (1991) Inner membrane protease 1, an enzyme mediating intramitochondrial protein sorting in yeast. EMBO J. 10: 247-254
    • (1991) EMBO J. , vol.10 , pp. 247-254
    • Schneider, A.1    Behrens, M.2    Scherer, P.3    Pratje, E.4    Michaelis, G.5    Schatz, G.6
  • 65
    • 0031964126 scopus 로고    scopus 로고
    • Feature-extraction from endopeptidase cleavage sites in mitochondrial targeting peptides
    • Schneider G, Sjöling S, Wallin E, Wrede P, Glaser E, von Heijne G (1998) Feature-extraction from endopeptidase cleavage sites in mitochondrial targeting peptides. Proteins 30: 49-60
    • (1998) Proteins , vol.30 , pp. 49-60
    • Schneider, G.1    Sjöling, S.2    Wallin, E.3    Wrede, P.4    Glaser, E.5    Von Heijne, G.6
  • 67
    • 0032055781 scopus 로고    scopus 로고
    • Mitochondrial targeting peptides in plants
    • Sjöling S, Glaser E (1998) Mitochondrial targeting peptides in plants. Trends Plant Sci 3: 136-140
    • (1998) Trends Plant Sci , vol.3 , pp. 136-140
    • Sjöling, S.1    Glaser, E.2
  • 68
    • 0026502349 scopus 로고
    • Mapping of the protein import machinery in the mitochondrial outer membrane by crosslinking of translocation intermediates
    • Söllner T, Rassow J, Wiedmann M, Schloßmann J, Keil P, Neupert W, Pfanner N (1992) Mapping of the protein import machinery in the mitochondrial outer membrane by crosslinking of translocation intermediates. Nature 355: 84-87
    • (1992) Nature , vol.355 , pp. 84-87
    • Söllner, T.1    Rassow, J.2    Wiedmann, M.3    Schloßmann, J.4    Keil, P.5    Neupert, W.6    Pfanner, N.7
  • 69
    • 0028009141 scopus 로고
    • RNA editing of a conserved reading frame in plant mitochondria increases its similarity to two overlapping reading frames in Escherichia coli
    • Sünkel S, Brennicke A, Knoop V (1994) RNA editing of a conserved reading frame in plant mitochondria increases its similarity to two overlapping reading frames in Escherichia coli. Mol. Gen. Genet. 242: 65-72
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 65-72
    • Sünkel, S.1    Brennicke, A.2    Knoop, V.3
  • 71
    • 0026660875 scopus 로고
    • Purification, cDNA cloning and Northern-blot analysis of the mitochondrial chaperonin 60 from pumpkin cotyledons
    • Tsugeki R, Mori H, Nishimura M (1992) Purification, cDNA cloning and Northern-blot analysis of the mitochondrial chaperonin 60 from pumpkin cotyledons. Eur. J. Biochem. 209: 453-458
    • (1992) Eur. J. Biochem. , vol.209 , pp. 453-458
    • Tsugeki, R.1    Mori, H.2    Nishimura, M.3
  • 72
    • 0031021278 scopus 로고    scopus 로고
    • The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides
    • Unseld M, Marienfeld JR, Brandt P, Brennicke A (1997) The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides. Nature Genetics 15: 57-61
    • (1997) Nature Genetics , vol.15 , pp. 57-61
    • Unseld, M.1    Marienfeld, J.R.2    Brandt, P.3    Brennicke, A.4
  • 73
    • 0027352972 scopus 로고
    • Molecular characterization of a 70 kDa heat-shock protein of bean mitochondria
    • Vidal V, Ranty B, Dillenschneider M, Charpenteau M, Ranjeva R (1993) Molecular characterization of a 70 kDa heat-shock protein of bean mitochondria. Plant J. 3: 143-150
    • (1993) Plant J. , vol.3 , pp. 143-150
    • Vidal, V.1    Ranty, B.2    Dillenschneider, M.3    Charpenteau, M.4    Ranjeva, R.5
  • 74
    • 0029868470 scopus 로고    scopus 로고
    • Phosphorylation of the transit sequence of chloroplast precursor proteins
    • Waegemann K, Soll J (1996) Phosphorylation of the transit sequence of chloroplast precursor proteins. J Biol Chem 271: 6545-6554
    • (1996) J Biol Chem , vol.271 , pp. 6545-6554
    • Waegemann, K.1    Soll, J.2
  • 75
    • 0026450340 scopus 로고
    • Characterization of PHSP1, a cDNA encoding a mitochondrial HSP70 from Pisum sativum
    • Watts FZ, Walters AJ, Moore AL (1992) Characterization of PHSP1, a cDNA encoding a mitochondrial HSP70 from Pisum sativum. Plant Mol. Biol. 18: 23-32
    • (1992) Plant Mol. Biol. , vol.18 , pp. 23-32
    • Watts, F.Z.1    Walters, A.J.2    Moore, A.L.3
  • 77
    • 0032563337 scopus 로고    scopus 로고
    • Targeting signals for a bacterial Sec-independent export system direct plant thylakoid import by the delta pH pathway
    • Wexler M, Bogsch EG, Klösgen RB, Palmer T, Robinson C, Berks BC (1998) Targeting signals for a bacterial Sec-independent export system direct plant thylakoid import by the delta pH pathway. FEBS Lett. 24: 339-342
    • (1998) FEBS Lett. , vol.24 , pp. 339-342
    • Wexler, M.1    Bogsch, E.G.2    Klösgen, R.B.3    Palmer, T.4    Robinson, C.5    Berks, B.C.6
  • 78
    • 0041113150 scopus 로고    scopus 로고
    • Overexpression of the mitochondrial matrix located HSP70 in transgenic tobacco results in enhanced growth characteristics
    • Moller IM, Gardeström P, Glimelius K, Glaser E (eds) Blackhuys Publishers, Leiden
    • Wood CK, Affourtit C, Albury MS, Carre J, Dudley P, Gordon J, Harpham NVJ, Whitehouse DG, Moore AL (1998) Overexpression of the mitochondrial matrix located HSP70 in transgenic tobacco results in enhanced growth characteristics. In: Moller IM, Gardeström P, Glimelius K, Glaser E (eds) Plant mitochondria: from gene to function. Blackhuys Publishers, Leiden, pp 211-217
    • (1998) Plant Mitochondria: From Gene to Function , pp. 211-217
    • Wood, C.K.1    Affourtit, C.2    Albury, M.S.3    Carre, J.4    Dudley, P.5    Gordon, J.6    Harpham, N.V.J.7    Whitehouse, D.G.8    Moore, A.L.9
  • 79
    • 0032825802 scopus 로고    scopus 로고
    • Planta (1999) 209: 275-281
    • (1999) , vol.209 , pp. 275-281


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