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Volumn 7, Issue 5, 1998, Pages 1186-1194

Isolation and characterization of a DnaJ-like protein in rats: The C- terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP- hydrolytic activity of hsc70 by a DnaJ-like protein

Author keywords

ATPase of hsc70; DnaJ homolog; Molecular chaperone; Protein protein interaction

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN 70; PROTEIN DERIVATIVE;

EID: 0031807387     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070513     Document Type: Article
Times cited : (10)

References (48)
  • 1
    • 0026569763 scopus 로고
    • MAS5, a yeast homolog of DnaJ involved in mitochondrial protein import
    • Atencio DP, Yaffe MP. 1992. MAS5, a yeast homolog of DnaJ involved in mitochondrial protein import. Mol Cell Biol 12:283-291.
    • (1992) Mol Cell Biol , vol.12 , pp. 283-291
    • Atencio, D.P.1    Yaffe, M.P.2
  • 3
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann RP, Mizzcn LA, Welch WJ. 1990. Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly. Science 248:850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzcn, L.A.2    Welch, W.J.3
  • 4
    • 0029911522 scopus 로고    scopus 로고
    • The cysteine string secretory vesicle protein activates Hsc70 ATPase
    • Braun JEA, Wilbanks SM, Scheller RH. 1996. The cysteine string secretory vesicle protein activates Hsc70 ATPase. J Biol Chem 271:25989-25993.
    • (1996) J Biol Chem , vol.271 , pp. 25989-25993
    • Braun, J.E.A.1    Wilbanks, S.M.2    Scheller, R.H.3
  • 5
    • 0027102871 scopus 로고
    • YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism
    • Caplan AJ, Cyr DM, Douglas MG. 1992. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71:1143-1155.
    • (1992) Cell , vol.71 , pp. 1143-1155
    • Caplan, A.J.1    Cyr, D.M.2    Douglas, M.G.3
  • 6
    • 0027308741 scopus 로고
    • Eukaryotic homologues of Escherichia coli dnaJ: A diverse protein family that functions with hsp70 stress proteins
    • Caplan AJ, Cyr DM, Douglas MG. 1993. Eukaryotic homologues of Escherichia coli dnaJ: A diverse protein family that functions with hsp70 stress proteins. Mol Biol Cell 4:555-563.
    • (1993) Mol Biol Cell , vol.4 , pp. 555-563
    • Caplan, A.J.1    Cyr, D.M.2    Douglas, M.G.3
  • 7
    • 0025745326 scopus 로고
    • Characterization of YDJ1 : A yeast homologue of the bacterial dnaJ protein
    • Caplan AJ, Douglas MG. 1991. Characterization of YDJ1 : A yeast homologue of the bacterial dnaJ protein. J Cell Biol 114:609-621.
    • (1991) J Cell Biol , vol.114 , pp. 609-621
    • Caplan, A.J.1    Douglas, M.G.2
  • 9
    • 0028099817 scopus 로고
    • Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b
    • Cheetham ME, Jackson AP, Anderton BH. 1994. Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b. Eur J Biochem 226:99-107.
    • (1994) Eur J Biochem , vol.226 , pp. 99-107
    • Cheetham, M.E.1    Jackson, A.P.2    Anderton, B.H.3
  • 10
    • 0027216523 scopus 로고
    • Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein
    • Chellaiah A, Davis A, Mohanakumar T. 1993. Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein. Biochim Biophys Acta 1174:111-113.
    • (1993) Biochim Biophys Acta , vol.1174 , pp. 111-113
    • Chellaiah, A.1    Davis, A.2    Mohanakumar, T.3
  • 11
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin JM, Przybyla AE, MacDonald RJ, Rutter WJ. 1979. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18:5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 12
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr DM, Langer T, Douglas MG. 1994. DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19:176-181.
    • (1994) Trends Biochem Sci , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 13
    • 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
  • 14
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty KM, DeLuca-Flaherty C, McKay DB. 1990. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346:623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    Deluca-Flaherty, C.2    McKay, D.B.3
  • 15
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysts of protein assembly
    • Flynn GC, Chappell TG, Rothman JE. 1989. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245:385-390.
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 16
    • 0028149893 scopus 로고
    • Common and divergent peptide binding specificities of hsp70 molecular chaperones
    • Fourie AM, Sambrook JF, Gething M-J. 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
  • 17
    • 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
  • 18
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman J, Nimmesgem E, Ohtsuka K, Hartl FU. 1994. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370:111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgem, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 19
    • 0026733631 scopus 로고
    • The emergence of the chaperone machines
    • Georgopoulos C. 1992. The emergence of the chaperone machines. Trends Biochem Sci 17:295-299.
    • (1992) Trends Biochem Sci , vol.17 , pp. 295-299
    • Georgopoulos, C.1
  • 20
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos C, Welch WJ. 1993. Role of the major heat shock proteins as molecular chaperones. Anna Rev Cell Biol 9:601-634.
    • (1993) Anna Rev Cell Biol , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 21
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M-J, Sambrook J. 1992. Protein folding in the cell. Nature 355:33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 22
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 23
    • 0027425585 scopus 로고
    • Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
    • Hendrick JP, Langer T, Davis TA, Hartl FU, Wiedmann M. 1993. Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc Natl Acad Sci USA 90:10216-10220.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10216-10220
    • Hendrick, J.P.1    Langer, T.2    Davis, T.A.3    Hartl, F.U.4    Wiedmann, M.5
  • 24
    • 0030220413 scopus 로고    scopus 로고
    • Involvement of the 10-kDa C-terminal fragment of hsc70 in complexing with unfolded protein
    • Hu SM, Wang C. 1996. Involvement of the 10-kDa C-terminal fragment of hsc70 in complexing with unfolded protein. Arch Biochem Biophys 332:163-169.
    • (1996) Arch Biochem Biophys , vol.332 , pp. 163-169
    • Hu, S.M.1    Wang, C.2
  • 25
    • 0027519155 scopus 로고
    • Aspartyl residue 10 is essential for ATPase activity of rat hsc70
    • Huang SP, Tsai MY, Tzou YM, Wu WG, Wang C. 1993. Aspartyl residue 10 is essential for ATPase activity of rat hsc70. J Biol Chem 268:2063-2068.
    • (1993) J Biol Chem , vol.268 , pp. 2063-2068
    • Huang, S.P.1    Tsai, M.Y.2    Tzou, Y.M.3    Wu, W.G.4    Wang, C.5
  • 26
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU. 1992. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356:683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 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
    • 0029741321 scopus 로고    scopus 로고
    • Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40
    • Minami Y, Hohfeld J, Ohtsuka K, Hartl FU. 1996. Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40. J Biol Chem 271:19617-19624.
    • (1996) J Biol Chem , vol.271 , pp. 19617-19624
    • Minami, Y.1    Hohfeld, J.2    Ohtsuka, K.3    Hartl, F.U.4
  • 29
    • 0027254681 scopus 로고
    • Human cDNA encoding DnaJ protein homologue
    • Oh S, Iwahori A, Kato S. 1993. Human cDNA encoding DnaJ protein homologue. Biochim Biophys Acta 1174:114-116.
    • (1993) Biochim Biophys Acta , vol.1174 , pp. 114-116
    • Oh, S.1    Iwahori, A.2    Kato, S.3
  • 30
    • 0027486385 scopus 로고
    • Cloning of a cDNa for heat-shock protein hsp40, a human homologue of bacterial DnaJ
    • Ohtsuka K. 1993. Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ. Biochem Biophvs Res Commun 197:235-240.
    • (1993) Biochem Biophvs Res Commun , vol.197 , pp. 235-240
    • Ohtsuka, K.1
  • 31
    • 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
  • 32
    • 0000675009 scopus 로고
    • Heat shock proteins and stress tolerance
    • Morimoto RI, Tessieres A, Georgopoulos C, eds. New York: Cold Spring Harbor Laboratory
    • Parsell DA, Lindquist S. 1994. Heat shock proteins and stress tolerance. In: Morimoto RI, Tessieres A, Georgopoulos C, eds. The biology of heat shock proteins and molecular chaperones. New York: Cold Spring Harbor Laboratory. pp 457-494.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 457-494
    • Parsell, D.A.1    Lindquist, S.2
  • 33
    • 0030581175 scopus 로고    scopus 로고
    • NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wuthrich K. 1996. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J Mol Biol 260:236-250.
    • (1996) J Mol Biol , vol.260 , pp. 236-250
    • Pellecchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wuthrich, K.5
  • 34
    • 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
  • 35
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 36
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schroder H, Langer T, Hartl FU, Bukau B. 1993. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J 12:4137-4144.
    • (1993) EMBO J , vol.12 , pp. 4137-4144
    • Schroder, H.1    Langer, T.2    Hartl, F.U.3    Bukau, B.4
  • 38
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling CJ, Rothblatt J, Hosobuchi M, Deshaies R, Schekman R. 1992. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol Biol Cell 3:129-142.
    • (1992) Mol Biol Cell , vol.3 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 39
    • 0030030946 scopus 로고    scopus 로고
    • A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
    • Szabo A, Korszun R, Hartl FU, Flanagan J. 1996. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J 15:408-417.
    • (1996) EMBO J , vol.15 , pp. 408-417
    • Szabo, A.1    Korszun, R.2    Hartl, F.U.3    Flanagan, J.4
  • 40
    • 0027987996 scopus 로고
    • NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain
    • Szyperski T, Pellecchia M, Wall D, Georgopoulos C, Wuthrich K. 1994. NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. Proc Natl Acad Sci USA 91:11343-11347.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11343-11347
    • Szyperski, T.1    Pellecchia, M.2    Wall, D.3    Georgopoulos, C.4    Wuthrich, K.5
  • 41
    • 0027989825 scopus 로고
    • Uncoupling of peptide-stimulated ATPase and clathrin-uncoating activity in deletion mutant of hsc70
    • Tsai MY, Wang C. 1994. Uncoupling of peptide-stimulated ATPase and clathrin-uncoating activity in deletion mutant of hsc70. J Biol Chem 269:5958-5962.
    • (1994) J Biol Chem , vol.269 , pp. 5958-5962
    • Tsai, M.Y.1    Wang, C.2
  • 42
    • 0028170215 scopus 로고
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication. J Biol Chem 269:5446-5451.
    • (1994) J Biol Chem , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 43
    • 0027433805 scopus 로고
    • Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding
    • Wang TF, Chang J-H, Wang C. 1993. Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding. J Biol Chem 268:26049-26051.
    • (1993) J Biol Chem , vol.268 , pp. 26049-26051
    • Wang, T.F.1    Chang, J.-H.2    Wang, C.3
  • 44
    • 0027179488 scopus 로고
    • High-level expression of soluble rat hsc70 in Escherichia coli: Purification and characterisation of the cloned enzyme
    • Wang C, Lee MR. 1993. High-level expression of soluble rat hsc70 in Escherichia coli: Purification and characterisation of the cloned enzyme. Biochem J 294:69-77.
    • (1993) Biochem J , vol.294 , pp. 69-77
    • Wang, C.1    Lee, M.R.2
  • 45
    • 0029094250 scopus 로고
    • Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates
    • Wawrzynow A, Zylicz M. 1995. Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. J Biol Chem 270:19300-19306.
    • (1995) J Biol Chem , vol.270 , pp. 19300-19306
    • Wawrzynow, A.1    Zylicz, M.2
  • 46
    • 0029922010 scopus 로고    scopus 로고
    • Rat kidney glutathione S-transferase 1 subunits have C-terminal truncations
    • Yeh HI, Lee JY, Tsai SP, Hsieh CH, Tam MF. 1996. Rat kidney glutathione S-transferase 1 subunits have C-terminal truncations. Biochem J 314:1017-1025.
    • (1996) Biochem J , vol.314 , pp. 1017-1025
    • Yeh, H.I.1    Lee, J.Y.2    Tsai, S.P.3    Hsieh, C.H.4    Tam, M.F.5
  • 47
    • 0029831050 scopus 로고    scopus 로고
    • Identification of elements of the peptide binding site of DnaK by peptide cross-linking
    • Zhang J, Walker GC. 1996. Identification of elements of the peptide binding site of DnaK by peptide cross-linking. J Biol Chem 271:19668-19674.
    • (1996) J Biol Chem , vol.271 , pp. 19668-19674
    • Zhang, J.1    Walker, G.C.2


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