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Volumn 5, Issue 1, 2000, Pages 62-71

In vivo and in vitro interaction of DnaK and a chloroplast transit peptide

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GLUTATHIONE TRANSFERASE; HEAT SHOCK PROTEIN 70; HYBRID PROTEIN; PROTEIN DNAK; RIBULOSEBISPHOSPHATE CARBOXYLASE; VEGETABLE PROTEIN;

EID: 0033968437     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(2000)005<0062:IVAIVI>2.0.CO;2     Document Type: Article
Times cited : (36)

References (50)
  • 3
    • 0028822223 scopus 로고
    • BiP and Sec63p are required for both co-and posttranslational protein translocation into the yeast endoplasmic reticulum
    • Brodsky JL, Goeckeler J, Schekman R. 1995. BiP and Sec63p are required for both co-and posttranslational protein translocation into the yeast endoplasmic reticulum. Proc Natl Acad Sci U S A 92: 9643-9646.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9643-9646
    • Brodsky, J.L.1    Goeckeler, J.2    Schekman, R.3
  • 4
    • 0032169930 scopus 로고    scopus 로고
    • The role of lipids in plastid protein transport
    • Bruce BD. 1998. The role of lipids in plastid protein transport. Plant Mol Biol 38: 223-246.
    • (1998) Plant Mol Biol , vol.38 , pp. 223-246
    • Bruce, B.D.1
  • 6
    • 0030918441 scopus 로고    scopus 로고
    • A folded protein can be transported across the chloroplast envelope and thylakoid membranes
    • Clark SA, Theg SM. 1997. A folded protein can be transported across the chloroplast envelope and thylakoid membranes. Mol Biol Cell 8: 923-934.
    • (1997) Mol Biol Cell , vol.8 , pp. 923-934
    • Clark, S.A.1    Theg, S.M.2
  • 8
    • 0026739395 scopus 로고
    • Regulation of Hsp70 function by a eukaryotic DnaJ homolog
    • Cyr DM, Lu X, Douglas MG. 1992. Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J Biol Chem 267: 20927-20931.
    • (1992) J Biol Chem , vol.267 , pp. 20927-20931
    • Cyr, D.M.1    Lu, X.2    Douglas, M.G.3
  • 9
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers M, Schatz G. 1986. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature 322: 228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 10
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman BC, Myers MP, Schumacher R, Morimoto RI. 1995. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J 14: 2281-2292.
    • (1995) EMBO J , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 12
    • 0029038943 scopus 로고
    • Protein translocation across chloroplast envelope membranes
    • Gray J, Row P. 1995. Protein translocation across chloroplast envelope membranes. Trends Cell Biol 5: 243-247.
    • (1995) Trends Cell Biol , vol.5 , pp. 243-247
    • Gray, J.1    Row, P.2
  • 13
    • 0027674916 scopus 로고
    • A strong protein unfolding activity is associated with the binding of precursor chloroplast proteins to chloroplast envelopes
    • Guera A, America T, van Waas M, Weisbeek PJ. 1993. A strong protein unfolding activity is associated with the binding of precursor chloroplast proteins to chloroplast envelopes. Plant Mol Biol 23: 309-324.
    • (1993) Plant Mol Biol , vol.23 , pp. 309-324
    • Guera, A.1    America, T.2    Van Waas, M.3    Weisbeek, P.J.4
  • 14
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl FU, Kuriyan J. 1997. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276: 431-435
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.U.4    Kuriyan, J.5
  • 15
    • 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
  • 16
    • 0022599858 scopus 로고
    • Transit peptides of nuclear-encoded chloroplast proteins share a common amino acid framework
    • Karlin Neumann GA, Tobin EM. 1986. Transit peptides of nuclear-encoded chloroplast proteins share a common amino acid framework. EMBO J 5: 9-13.
    • (1986) EMBO J , vol.5 , pp. 9-13
    • Karlin Neumann, G.A.1    Tobin, E.M.2
  • 18
    • 0027512825 scopus 로고
    • Ribonuclease S-peptide as a carrier in fusion proteins
    • Kim JS, Raines RT. 1993. Ribonuclease S-peptide as a carrier in fusion proteins. Protein Sci 2: 348-356.
    • (1993) Protein Sci , vol.2 , pp. 348-356
    • Kim, J.S.1    Raines, R.T.2
  • 19
    • 0032190144 scopus 로고    scopus 로고
    • Amino-terminal and hydrophobic regions of the Chlamydomonas reinhardtii plastocyanin transit peptide are required for efficient protein accumulation in vivo
    • Kindle KL. 1998. Amino-terminal and hydrophobic regions of the Chlamydomonas reinhardtii plastocyanin transit peptide are required for efficient protein accumulation in vivo. Plant Mol Biol 38: 365-377.
    • (1998) Plant Mol Biol , vol.38 , pp. 365-377
    • Kindle, K.L.1
  • 20
    • 0029118986 scopus 로고
    • Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP
    • King C, Eisenberg E, Greene L. 1995. Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP. J Biol Chem 270: 22535-22540.
    • (1995) J Biol Chem , vol.270 , pp. 22535-22540
    • King, C.1    Eisenberg, E.2    Greene, L.3
  • 21
    • 0029974513 scopus 로고    scopus 로고
    • Determinants in the presequence of cytochrome b2 for import into mitochondria and for proteolytic processing
    • Klaus C, Guiard B, Neupert W, Brunner M. 1996. Determinants in the presequence of cytochrome b2 for import into mitochondria and for proteolytic processing. Eur J Biochem 236: 856-861.
    • (1996) Eur J Biochem , vol.236 , pp. 856-861
    • Klaus, C.1    Guiard, B.2    Neupert, W.3    Brunner, M.4
  • 22
    • 0026744686 scopus 로고
    • Isolation and characterization of a cDNA clone encoding a cognate 70-kDa heat shock protein of the chloroplast envelope
    • Ko K, Bornemisza O, Kourtz L, Ko ZW, Plaxton WC, Cashmore AR. 1992. Isolation and characterization of a cDNA clone encoding a cognate 70-kDa heat shock protein of the chloroplast envelope. J Biol Chem 267: 2986-2993.
    • (1992) J Biol Chem , vol.267 , pp. 2986-2993
    • Ko, K.1    Bornemisza, O.2    Kourtz, L.3    Ko, Z.W.4    Plaxton, W.C.5    Cashmore, A.R.6
  • 23
    • 0031034588 scopus 로고    scopus 로고
    • The early stage of chloroplast protein import involves Com70
    • Kourtz L, Ko K. 1997. The early stage of chloroplast protein import involves Com70. J Biol Chem 272: 2808-2813.
    • (1997) J Biol Chem , vol.272 , pp. 2808-2813
    • Kourtz, L.1    Ko, K.2
  • 24
    • 0028276219 scopus 로고
    • The binding of substrates and inhibitors to the metal center of myoinositol monophosphatase
    • Kwok F, Churchich JE. 1994. The binding of substrates and inhibitors to the metal center of myoinositol monophosphatase. FEBS Lett 346: 304-306.
    • (1994) FEBS Lett , vol.346 , pp. 304-306
    • Kwok, F.1    Churchich, J.E.2
  • 25
    • 0026320296 scopus 로고
    • The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein
    • Liberek K, Skowyra D, Zylicz M, Johnson C, Georgopoulos C. 1991. The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. J Biol Chem 266: 14491-14496.
    • (1991) J Biol Chem , vol.266 , pp. 14491-14496
    • Liberek, K.1    Skowyra, D.2    Zylicz, M.3    Johnson, C.4    Georgopoulos, C.5
  • 27
    • 0001734650 scopus 로고
    • Isolation and characterization of a cDNA clone encoding the major Hsp70 of the pea chloroplastic stroma
    • Marshall JS, Keegstra K. 1992. Isolation and characterization of a cDNA clone encoding the major Hsp70 of the pea chloroplastic stroma. Plant Physiol 100: 1048-1054.
    • (1992) Plant Physiol , vol.100 , pp. 1048-1054
    • Marshall, J.S.1    Keegstra, K.2
  • 28
    • 0000636482 scopus 로고
    • Endopeptidases in the stroma and thylakoids of pea chloroplasts
    • Musgrove JE, Elderfield PD, Robinson C. 1989. Endopeptidases in the stroma and thylakoids of pea chloroplasts. Plant Physiol 90: 1616-1621.
    • (1989) Plant Physiol , vol.90 , pp. 1616-1621
    • Musgrove, J.E.1    Elderfield, P.D.2    Robinson, C.3
  • 29
    • 0031048279 scopus 로고    scopus 로고
    • Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone
    • Nielsen E, Akita M, Davila-Aponte J, Keegstra K. 1997. Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone. EMBO J 16: 935-946.
    • (1997) EMBO J , vol.16 , pp. 935-946
    • Nielsen, E.1    Akita, M.2    Davila-Aponte, J.3    Keegstra, K.4
  • 30
    • 0025667283 scopus 로고
    • Precursor proteins in transit through mitochondrial contact sites interact with hsp70 in the matrix
    • Ostermann J, Voos W, Kang PJ, Craig EA, Neupert W, Pfanner N. 1990. Precursor proteins in transit through mitochondrial contact sites interact with hsp70 in the matrix. FEBS Lett 277: 281-284.
    • (1990) FEBS Lett , vol.277 , pp. 281-284
    • Ostermann, J.1    Voos, W.2    Kang, P.J.3    Craig, E.A.4    Neupert, W.5    Pfanner, N.6
  • 31
    • 0027418663 scopus 로고
    • Conformational change of chaperone Hsc70 upon binding to a decapeptide: A circular dichroism study
    • Park K, Flynn CC, Rothman JE, Fasman GD. 1993. Conformational change of chaperone Hsc70 upon binding to a decapeptide: a circular dichroism study. Protein Sci 2: 325-330.
    • (1993) Protein Sci , vol.2 , pp. 325-330
    • Park, K.1    Flynn, C.C.2    Rothman, J.E.3    Fasman, G.D.4
  • 32
    • 0028926428 scopus 로고
    • Functional domains of the ferredoxin transit sequence involved in chloroplast import
    • Pilon M, Wienk H, Sips W, et al. 1995. Functional domains of the ferredoxin transit sequence involved in chloroplast import. J Biol Chem 270: 3882-3893.
    • (1995) J Biol Chem , vol.270 , pp. 3882-3893
    • Pilon, M.1    Wienk, H.2    Sips, W.3
  • 33
    • 0030472762 scopus 로고    scopus 로고
    • In vitro interaction between a chloroplast transit peptide and chloroplast outer envelope lipids is sequence-specific and lipid class-dependent
    • Pinnaduwage P, Bruce BD. 1996. In vitro interaction between a chloroplast transit peptide and chloroplast outer envelope lipids is sequence-specific and lipid class-dependent. J Biol Chem 271: 32907-32915.
    • (1996) J Biol Chem , vol.271 , pp. 32907-32915
    • Pinnaduwage, P.1    Bruce, B.D.2
  • 34
    • 0032187868 scopus 로고    scopus 로고
    • Domains of a transit sequence required for in vivo import in Arabidopsis chloroplasts
    • Rensink WA, Pilon M, Weisbeek P. 1998. Domains of a transit sequence required for in vivo import in Arabidopsis chloroplasts. Plant Physiol 118: 691-699.
    • (1998) Plant Physiol , vol.118 , pp. 691-699
    • Rensink, W.A.1    Pilon, M.2    Weisbeek, P.3
  • 35
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rudiger S, Germeroth L, Schneider-Mergener J, Bukau B. 1997. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J 16: 1501-1507.
    • (1997) EMBO J , vol.16 , pp. 1501-1507
    • Rudiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 36
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G, Dobberstein B. 1996. Common principles of protein translocation across membranes. Science 271: 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 37
    • 0025673942 scopus 로고
    • A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein
    • Scherer PE, Krieg UC, Hwang ST, Vestweber D, Schatz G. 1990. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein. EMBO J 9: 4315-4322.
    • (1990) EMBO J , vol.9 , pp. 4315-4322
    • Scherer, P.E.1    Krieg, U.C.2    Hwang, S.T.3    Vestweber, D.4    Schatz, G.5
  • 38
    • 0030026850 scopus 로고    scopus 로고
    • Molecular chaperones are present in the thylakoid lumen of pea chloroplasts
    • Schlicher T, Soll J. 1996. Molecular chaperones are present in the thylakoid lumen of pea chloroplasts. FEBS Lett 379: 302-304.
    • (1996) FEBS Lett , vol.379 , pp. 302-304
    • Schlicher, T.1    Soll, J.2
  • 39
    • 0026697941 scopus 로고
    • Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK
    • Schmid D, Jaussi R, Christen P. 1992. Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK. Eur J Biochem 208: 699-704.
    • (1992) Eur J Biochem , vol.208 , pp. 699-704
    • Schmid, D.1    Jaussi, R.2    Christen, P.3
  • 40
    • 0028109712 scopus 로고
    • Isolation of components of the chloroplast protein import machinery
    • Schnell DJ, Kessler F, Blobel G. 1994. Isolation of components of the chloroplast protein import machinery. Science 266: 1007-1012.
    • (1994) Science , vol.266 , pp. 1007-1012
    • Schnell, D.J.1    Kessler, F.2    Blobel, G.3
  • 41
    • 0028929052 scopus 로고
    • The DnaK chaperone system of Escherichia coli: Quaternary structures and interactions of the DnaK and GrpE components
    • Schonfeld HJ, Schmidt D, Schroder H, Bukau B. 1995. The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components. J Biol Chem 270: 2183-2189.
    • (1995) J Biol Chem , vol.270 , pp. 2183-2189
    • Schonfeld, H.J.1    Schmidt, D.2    Schroder, H.3    Bukau, B.4
  • 42
    • 0030067134 scopus 로고    scopus 로고
    • A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: Energetics and mechanistic implications
    • Scott SV, Theg SM. 1996. A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: energetics and mechanistic implications. J Cell Biol 132: 63-75.
    • (1996) J Cell Biol , vol.132 , pp. 63-75
    • Scott, S.V.1    Theg, S.M.2
  • 43
    • 0025885725 scopus 로고
    • Formation in vitro of complexes between an abnormal fusion protein and the heat shock proteins from Escherichia coli and yeast mitochondria
    • Sherman MY, Goldberg AL. 1991. Formation in vitro of complexes between an abnormal fusion protein and the heat shock proteins from Escherichia coli and yeast mitochondria. J Bacteriol 173: 7249-7256.
    • (1991) J Bacteriol , vol.173 , pp. 7249-7256
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 44
    • 0000687843 scopus 로고
    • A functionally active protein import complex from chloroplasts
    • Soll J, Waegemann K. 1992. A functionally active protein import complex from chloroplasts. Plant J Oxford 2: 253-256.
    • (1992) Plant J Oxford , vol.2 , pp. 253-256
    • Soll, J.1    Waegemann, K.2
  • 45
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
    • Szabo A, Langer T, Schroder H, Flanagan J, Bukau B, Hartl FU. 1994. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc Natl Acad Sci U S A 91: 10345-10349.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schroder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.U.6
  • 46
    • 0024202929 scopus 로고
    • A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites
    • Vestweber D, Schatz G. 1988. A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites. J Cell Biol 107: 2037-2043.
    • (1988) J Cell Biol , vol.107 , pp. 2037-2043
    • Vestweber, D.1    Schatz, G.2
  • 48
    • 0026097503 scopus 로고
    • Chloroplast transit peptides. The perfect random coil?
    • von Heijne G, Nishikawa K. 1991. Chloroplast transit peptides. The perfect random coil? FEBS Lett 278: 1-3.
    • (1991) FEBS Lett , vol.278 , pp. 1-3
    • Von Heijne, G.1    Nishikawa, K.2
  • 49
    • 0033597380 scopus 로고    scopus 로고
    • Interaction of mitochondrial presequences with DnaK and mitochondrial hsp70
    • Zhang XP, Elofsson A, Andreu D, Glaser E. 1999. Interaction of mitochondrial presequences with DnaK and mitochondrial hsp70. J Mol Biol 288: 177-190.
    • (1999) J Mol Biol , vol.288 , pp. 177-190
    • Zhang, X.P.1    Elofsson, A.2    Andreu, D.3    Glaser, E.4


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