메뉴 건너뛰기




Volumn 122, Issue 4, 2000, Pages 1289-1299

Identification of a Hsp70 recognition domain within the Rubisco small subunit transit peptide

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; CSS1 PROTEIN; GENE FUNCTION; HSP70 MOLECULAR CHAPERONE; MOLECULAR MODEL; MUTANT; PISUM SATIVUM; PROTEIN DNAK; PROTEIN PROTEIN INTERACTION; RIBULOSEBISPHOSPHATE CARBOXYLASE; SSTP PEPTIDE; STATISTICAL ANALYSIS; SYNTHETIC PEPTIDE; TRANSIT PEPTIDE;

EID: 0033996510     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.122.4.1289     Document Type: Article
Times cited : (86)

References (51)
  • 1
    • 0030896924 scopus 로고    scopus 로고
    • Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking
    • Akita M, Nielsen E, Keegstra K (1997) Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking. J Cell Biol 136: 983-994
    • (1997) J Cell Biol , vol.136 , pp. 983-994
    • Akita, M.1    Nielsen, E.2    Keegstra, K.3
  • 2
    • 0030841365 scopus 로고    scopus 로고
    • The mitochondrial hsp70 chaperone system: Effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70
    • Azem A, Oppliger W, Lustig A, Jeno P, Feifel B, Schatz G, Horst M (1997) The mitochondrial hsp70 chaperone system: effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70. J Biol Chem 272: 20901-20906
    • (1997) J Biol Chem , vol.272 , pp. 20901-20906
    • Azem, A.1    Oppliger, W.2    Lustig, A.3    Jeno, P.4    Feifel, B.5    Schatz, G.6    Horst, M.7
  • 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
    • 0002093629 scopus 로고
    • In vitro import of proteins into chloroplasts
    • Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Bruce BD, Perry S, Froehlich J, Keegstra K (1994) In vitro import of proteins into chloroplasts. In Plant Molecular Biology Manual. Kluwer Academic Publishers, Dordrecht, The Netherlands, pp 1-15
    • (1994) Plant Molecular Biology Manual , pp. 1-15
    • Bruce, B.D.1    Perry, S.2    Froehlich, J.3    Keegstra, K.4
  • 7
    • 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
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn GC, Pohl J, Flocco MT, Rothman JE (1991) Peptide-binding specificity of the molecular chaperone BiP. Nature 353: 726-730
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 10
    • 0028149893 scopus 로고
    • Common and divergent peptide binding specificities of hsp70 molecular chaperones
    • Fourie AM, Sambrook JF, Gething MJ (1994) Common and divergent peptide binding specificities of hsp70 molecular chaperones. J Biol Chem 269: 30470-30478
    • (1994) J Biol Chem , vol.269 , pp. 30470-30478
    • Fourie, A.M.1    Sambrook, J.F.2    Gething, M.J.3
  • 11
    • 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
    • 0032546762 scopus 로고    scopus 로고
    • Catapult mechanism renders the chaperone action of Hsp70 unidirectional
    • Gisler SM, Pierpaoli E V, Christen P (1998) Catapult mechanism renders the chaperone action of Hsp70 unidirectional. J Mol Biol 279: 833-840
    • (1998) J Mol Biol , vol.279 , pp. 833-840
    • Gisler, S.M.1    Pierpaoli, E.V.2    Christen, P.3
  • 13
    • 0028834046 scopus 로고
    • Can Hsp70 proteins act as force-generating motors?
    • Glick BS (1995) Can Hsp70 proteins act as force-generating motors? Cell 80: 11-14
    • (1995) Cell , vol.80 , pp. 11-14
    • Glick, B.S.1
  • 15
    • 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
  • 16
    • 0030098733 scopus 로고    scopus 로고
    • Degradation of mistargeted OEE33 in the chloroplast stroma
    • Halperin T, Adam Z (1996) Degradation of mistargeted OEE33 in the chloroplast stroma. Plant Mol Biol 30: 925-933
    • (1996) Plant Mol Biol , vol.30 , pp. 925-933
    • Halperin, T.1    Adam, Z.2
  • 17
    • 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
  • 18
    • 0028584270 scopus 로고
    • A receptor component of the chloroplast protein translocation machinery
    • Hirsch S, Muckel E, Heemeyer F, von Heijne G, Soll J (1994) A receptor component of the chloroplast protein translocation machinery. Science 266: 1989-1992
    • (1994) Science , vol.266 , pp. 1989-1992
    • Hirsch, S.1    Muckel, E.2    Heemeyer, F.3    Von Heijne, G.4    Soll, J.5
  • 19
    • 0033968437 scopus 로고    scopus 로고
    • In vivo and in vitro interaction of DnaK and a chloroplast transit peptide
    • Ivey RA, Bruce BD (2000) In vivo and in vitro interaction of DnaK and a chloroplast transit peptide. Cell Stress Chaperones 5: 62-71
    • (2000) Cell Stress Chaperones , vol.5 , pp. 62-71
    • Ivey, R.A.1    Bruce, B.D.2
  • 20
    • 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
  • 22
    • 0027984260 scopus 로고
    • Identification of two GTP-binding proteins in the chloroplast protein import machinery
    • Kessler F, Blobel G, Patel HA, Schnell DJ (1994) Identification of two GTP-binding proteins in the chloroplast protein import machinery. Science 266: 1035-1039
    • (1994) Science , vol.266 , pp. 1035-1039
    • Kessler, F.1    Blobel, G.2    Patel, H.A.3    Schnell, D.J.4
  • 23
    • 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
  • 24
    • 0032539010 scopus 로고    scopus 로고
    • Tic20 and Tic22 are new components of the protein import apparatus at the chloroplast inner envelope membrane
    • Kouranov A, Chen X, Fuks B, Schnell DJ (1998) Tic20 and Tic22 are new components of the protein import apparatus at the chloroplast inner envelope membrane. J Cell Biol 143: 991-1002
    • (1998) J Cell Biol , vol.143 , pp. 991-1002
    • Kouranov, A.1    Chen, X.2    Fuks, B.3    Schnell, D.J.4
  • 25
    • 0033215007 scopus 로고    scopus 로고
    • A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii
    • Krimm I, Gans P, Hernandez JF, Arlaud GJ, Lancelin JM (1999) A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii. Eur J Biochem 265: 171-180
    • (1999) Eur J Biochem , vol.265 , pp. 171-180
    • Krimm, I.1    Gans, P.2    Hernandez, J.F.3    Arlaud, G.J.4    Lancelin, J.M.5
  • 26
    • 0028281852 scopus 로고
    • NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution
    • Lancelin JM, Bally I, Arlaud GJ, Blackledge M, Gans P, Stein M, Jacquot JP (1994) NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution. FEBS Lett 343: 261-266
    • (1994) FEBS Lett , vol.343 , pp. 261-266
    • Lancelin, J.M.1    Bally, I.2    Arlaud, G.J.3    Blackledge, M.4    Gans, P.5    Stein, M.6    Jacquot, J.P.7
  • 27
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci USA 88: 2874-2878
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 28
    • 0029775088 scopus 로고    scopus 로고
    • Topology of IEP110, a component of the chloroplastic protein import machinery present in the inner envelope membrane
    • Lubeck J, Soll J, Akita M, Nielsen E, Keegstra K (1996) Topology of IEP110, a component of the chloroplastic protein import machinery present in the inner envelope membrane. EMBO J 15: 4230-4238
    • (1996) EMBO J , vol.15 , pp. 4230-4238
    • Lubeck, J.1    Soll, J.2    Akita, M.3    Nielsen, E.4    Keegstra, K.5
  • 29
    • 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
  • 30
    • 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
  • 31
    • 0026768015 scopus 로고
    • DnaK, hsp73, and their molten globules: Two different ways heat shock proteins respond to heat
    • Palleros DR, Reid KL, McCarty JS, Walker GC, Fink AL (1992) DnaK, hsp73, and their molten globules: two different ways heat shock proteins respond to heat. J Biol Chem 267: 5279-5285
    • (1992) J Biol Chem , vol.267 , pp. 5279-5285
    • Palleros, D.R.1    Reid, K.L.2    McCarty, J.S.3    Walker, G.C.4    Fink, A.L.5
  • 32
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • Palleros DR, Welch WJ, Fink AL (1991) Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc Natl Acad Sci USA 88: 5719-5723
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 34
    • 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
  • 35
    • 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
  • 36
    • 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
  • 37
    • 0026799491 scopus 로고
    • Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange
    • Sadis S, Hightower LE (1992) Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry 31: 9406-9412
    • (1992) Biochemistry , vol.31 , pp. 9406-9412
    • Sadis, S.1    Hightower, L.E.2
  • 38
    • 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
  • 39
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: Purification of an uncoating ATPase
    • Schlossman DM, Schmid SL, Braell WA, Rothman JE (1984) An enzyme that removes clathrin coats: purification of an uncoating ATPase. J Cell Biol 99: 723-733
    • (1984) J Cell Biol , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.E.4
  • 40
    • 0029045002 scopus 로고
    • Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70
    • Schmitt M, Neupert W, Langer T (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14: 3434-3444
    • (1995) EMBO J , vol.14 , pp. 3434-3444
    • Schmitt, M.1    Neupert, W.2    Langer, T.3
  • 41
    • 0000103040 scopus 로고    scopus 로고
    • A consensus nomenclature for the protein-import components of the chloroplast envelope
    • Schnell DJ, Blobel G, Keegstra K, Kessler F, Ko K, Soll J (1997) A consensus nomenclature for the protein-import components of the chloroplast envelope. Trends Cell Biol 7: 303-304
    • (1997) Trends Cell Biol , vol.7 , pp. 303-304
    • Schnell, D.J.1    Blobel, G.2    Keegstra, K.3    Kessler, F.4    Ko, K.5    Soll, J.6
  • 42
    • 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
  • 43
    • 0029257229 scopus 로고
    • A constituent of the chloroplast import complex represents a new type of GTP-binding protein
    • Seedorf M, Waegemann K, Soll J (1995) A constituent of the chloroplast import complex represents a new type of GTP-binding protein. Plant J 7235: 401-411
    • (1995) Plant J , vol.7235 , pp. 401-411
    • Seedorf, M.1    Waegemann, K.2    Soll, J.3
  • 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 2: 253-256
    • (1992) Plant J , vol.2 , pp. 253-256
    • Soll, J.1    Waegemann, K.2
  • 46
    • 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
  • 47
    • 0000489161 scopus 로고
    • Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts
    • Waegemann K, Soll J (1991) Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts. Plant J 1: 149-158
    • (1991) Plant J , vol.1 , pp. 149-158
    • Waegemann, K.1    Soll, J.2
  • 48
    • 0032784582 scopus 로고    scopus 로고
    • The structural flexibility of the preferredoxin transit peptide
    • Wienk HLJ, Czisch M, de Kruijff B (1999) The structural flexibility of the preferredoxin transit peptide. FEBS Lett 453: 318-326
    • (1999) FEBS Lett , vol.453 , pp. 318-326
    • Wienk, H.L.J.1    Czisch, M.2    De Kruijff, B.3
  • 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
  • 51
    • 0028921261 scopus 로고
    • The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydjlp and peptide substrates
    • Ziegelhoffer T, Lopez-Buesa P, Craig EA (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydjlp and peptide substrates. J Biol Chem 270: 10412-10419
    • (1995) J Biol Chem , vol.270 , pp. 10412-10419
    • Ziegelhoffer, T.1    Lopez-Buesa, P.2    Craig, E.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.