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Volumn 286, Issue 3, 1999, Pages 915-932

Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling

Author keywords

Allosterism; Calorimetry; Chaperones; DnaK; Fluorescence

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; MUTANT PROTEIN; PROTEIN DNAK;

EID: 0033605086     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2514     Document Type: Article
Times cited : (133)

References (68)
  • 1
    • 0024978379 scopus 로고
    • Ordered assembly of nucleoprotein structures at the bacteriophage λ replication origin during the initiation of DNA replication
    • Alfano C., McMacken R. Ordered assembly of nucleoprotein structures at the bacteriophage λ replication origin during the initiation of DNA replication. J. Biol. Chem. 264:1989a;10699-10708.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10699-10708
    • Alfano, C.1    McMacken, R.2
  • 2
    • 0024978377 scopus 로고
    • Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage λ DNA replication
    • Alfano C., McMacken R. Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage λ DNA replication. J. Biol. Chem. 264:1989b;10709-10718.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10709-10718
    • Alfano, C.1    McMacken, R.2
  • 3
    • 0026491207 scopus 로고
    • Structural and functional relationships in DnaK and DnaK756 heat-shock proteins from Escherichia coli
    • Banecki B., Zylicz M., Bertoli E., Tanfani F. Structural and functional relationships in DnaK and DnaK756 heat-shock proteins from Escherichia coli. J. Biol. Chem. 267:1992;25051-25058.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25051-25058
    • Banecki, B.1    Zylicz, M.2    Bertoli, E.3    Tanfani, F.4
  • 4
    • 0025303147 scopus 로고
    • Interaction of Hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann R. P., Mizzen L. A., Welch W. J. Interaction of Hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science. 248:1990;850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 5
    • 0021471706 scopus 로고
    • Dissociation of clathrin coats coupled to the hydrolysis of ATP: Role of an uncoating ATPase
    • Braell W. A., Schlossman D. M., Schmid S. L., Rothman J. E. Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase. J. Cell. Biol. 99:1984;734-741.
    • (1984) J. Cell. Biol. , vol.99 , pp. 734-741
    • Braell, W.A.1    Schlossman, D.M.2    Schmid, S.L.3    Rothman, J.E.4
  • 6
    • 85047669331 scopus 로고    scopus 로고
    • Post-translational protein translocation: Not all hsc70s are created equal
    • Brodsky J. L. Post-translational protein translocation: not all hsc70s are created equal. Trends Biochem. Sci. 21:1996;122-126.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 122-126
    • Brodsky, J.L.1
  • 7
    • 0028297010 scopus 로고
    • The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171
    • Buchberger A., Valencia A., McMacken R., Sander C., Bukau B. The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J. 13:1994a;1687-1695.
    • (1994) EMBO J. , vol.13 , pp. 1687-1695
    • Buchberger, A.1    Valencia, A.2    McMacken, R.3    Sander, C.4    Bukau, B.5
  • 8
    • 0028382510 scopus 로고
    • A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE
    • Buchberger A., Schröder H., Büttner M., Valencia A., Bukau B. A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nature Struct. Biol. 1:1994b;95-101.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 95-101
    • Buchberger, A.1    Schröder, H.2    Büttner, M.3    Valencia, A.4    Bukau, B.5
  • 9
    • 0029037015 scopus 로고
    • Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication
    • Buchberger A., Theyssen H., Schröder H., McCarty J. S., Virgallita G., Milkereit P., Reinstein J., Bukau B. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem. 270:1995;16903-16910.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16903-16910
    • Buchberger, A.1    Theyssen, H.2    Schröder, H.3    McCarty, J.S.4    Virgallita, G.5    Milkereit, P.6    Reinstein, J.7    Bukau, B.8
  • 10
    • 0025048776 scopus 로고
    • Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone
    • Bukau B., Walker G. C. Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone. EMBO J. 9:1990;4027-4036.
    • (1990) EMBO J. , vol.9 , pp. 4027-4036
    • Bukau, B.1    Walker, G.C.2
  • 15
    • 0001880425 scopus 로고
    • Chemical properties of polypeptides
    • New York: W. H. Freeman and Company. p. 1-48
    • Creighton T. E. Chemical properties of polypeptides. Proteins: Structures and Molecular Properties. 1993;W. H. Freeman and Company, New York. p. 1-48.
    • (1993) Proteins: Structures and Molecular Properties
    • Creighton, T.E.1
  • 16
    • 0024978387 scopus 로고
    • Specialized nucleoprotein structures at the origin of replication of bacteriophage λ
    • Dodson M., McMacken R., Echols H. Specialized nucleoprotein structures at the origin of replication of bacteriophage λ J. Biol. Chem. 264:1989;10719-10725.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10719-10725
    • Dodson, M.1    McMacken, R.2    Echols, H.3
  • 17
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein
    • Flaherty K. M., DeLuca-Flaherty C., McKay D. B. Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein. Nature. 346:1990;623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 18
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysts of protein assembly
    • Flynn G. C., Chappell T. G., Rothman J. E. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science. 245:1989;385-390.
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 19
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman B. C., Morimoto R. I. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 15:1996;2969-2979.
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 20
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman B. C., Myers M. P., Schumacher R., Morimoto R. I. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14:1995;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
  • 21
    • 0002377439 scopus 로고
    • Properties of the Escherichia coli heat shock proteins and their role in bacteriophage λ growth
    • R. I. Morimoto, A. Tissieres, & C. Georgopoulos. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Georgopoulos C., Ang D., Liberek K., Zylicz M. Properties of the Escherichia coli heat shock proteins and their role in bacteriophage λ growth. Morimoto R. I., Tissieres A., Georgopoulos C. Stress Proteins in Biology and Medicine. 1990;191-221 Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1990) Stress Proteins in Biology and Medicine , pp. 191-221
    • Georgopoulos, C.1    Ang, D.2    Liberek, K.3    Zylicz, M.4
  • 23
    • 0030735086 scopus 로고    scopus 로고
    • Destabilization of peptide binding and interdomain communication by an E543 K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone
    • Ha J.-H., Hellman U., Johnson E. R., Li L., McKay D. B., Sousa M. C., Takeda S., Wernstedt C., Wilbanks S. M. Destabilization of peptide binding and interdomain communication by an E543 K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone. J. Biol. Chem. 272:1997;27796-27803.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27796-27803
    • Ha, J.-H.1    Hellman, U.2    Johnson, E.R.3    Li, L.4    McKay, D.B.5    Sousa, M.C.6    Takeda, S.7    Wernstedt, C.8    Wilbanks, S.M.9
  • 24
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison C. J., Hayer-Hartl M., Di Liberto M., Hartl F.-U., Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science. 276:1997;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
  • 25
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F. U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 26
    • 0028914392 scopus 로고
    • Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins
    • Jordan R., McMacken R. Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins. J. Biol. Chem. 270:1995;4563-4569.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4563-4569
    • Jordan, R.1    McMacken, R.2
  • 27
    • 13344281021 scopus 로고
    • Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes
    • Kamath-Loeb A. S., Lu C. Z., Suh W.-C., Lonetto M. A., Gross C. A. Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes. J. Biol. Chem. 270:1995;30051-30059.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30051-30059
    • Kamath-Loeb, A.S.1    Lu, C.Z.2    Suh, W.-C.3    Lonetto, M.A.4    Gross, C.A.5
  • 28
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang P. J., Ostermann J., Shilling J., Neupert W., Craig E. A., Pfanner N. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature. 348:1990;137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 29
    • 15844372190 scopus 로고    scopus 로고
    • A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
    • Karzai A. W., McMacken R. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271:1996;11236-11246.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11236-11246
    • Karzai, A.W.1    McMacken, R.2
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 0026595140 scopus 로고
    • Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
    • Landry S. J., Jordan R., McMacken R., Gierasch L. M. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature. 355:1992;455-457.
    • (1992) Nature , vol.355 , pp. 455-457
    • Landry, S.J.1    Jordan, R.2    McMacken, R.3    Gierasch, L.M.4
  • 33
    • 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 M. K., Hartl F. U. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature. 356:1992;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
  • 34
    • 0012749458 scopus 로고
    • Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage λ DNA replication
    • Liberek K., Georgopoulos C., Zylicz M. Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage λ DNA replication. Proc. Natl Acad. Sci. USA. 85:1988;6632-6636.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 6632-6636
    • Liberek, K.1    Georgopoulos, C.2    Zylicz, M.3
  • 35
    • 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. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl Acad. Sci. USA. 88:1991a;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
  • 36
    • 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. 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. 266:1991b;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
  • 37
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty J. S., Buchberger A., Reinstein J., Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249:1995;126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 38
    • 0024555841 scopus 로고
    • Reconstitution of a nine-protein system that initiates bacteriophage λ DNA replication
    • Mensa-Wilmot K., Seaby R., Alfano C., Wold M. S., Gomes B., McMacken R. Reconstitution of a nine-protein system that initiates bacteriophage λ DNA replication. J. Biol. Chem. 264:1989;2853-2861.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2853-2861
    • Mensa-Wilmot, K.1    Seaby, R.2    Alfano, C.3    Wold, M.S.4    Gomes, B.5    McMacken, R.6
  • 39
    • 0024430704 scopus 로고
    • Mutational analysis of the human HSP70 protein: Distinct domains for nucleolar localization and adenosine triphosphate binding
    • Milarski K. L., Morimoto R. I. Mutational analysis of the human HSP70 protein: distinct domains for nucleolar localization and adenosine triphosphate binding. J. Cell. Biol. 109:1989;1947-1962.
    • (1989) J. Cell. Biol. , vol.109 , pp. 1947-1962
    • Milarski, K.L.1    Morimoto, R.I.2
  • 40
    • 0026772142 scopus 로고
    • DNA sequence analysis of the dnaK gene of Escherichia coli B and of two dnaK genes carrying the temperature-sensitive mutations dnak7 (Ts) and dnaK756 (Ts)
    • Miyazaki T., Tanaka S., Fujita H., Itikawa H. DNA sequence analysis of the dnaK gene of Escherichia coli B and of two dnaK genes carrying the temperature-sensitive mutations dnak7 (Ts) and dnaK756 (Ts). J. Bacteriol. 174:1992;3715-3722.
    • (1992) J. Bacteriol. , vol.174 , pp. 3715-3722
    • Miyazaki, T.1    Tanaka, S.2    Fujita, H.3    Itikawa, H.4
  • 41
    • 0027172465 scopus 로고
    • Thermodynamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK
    • Montgomery D., Jordan R., McMacken R., Freire E. Thermodynamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK. J. Mol. Biol. 232:1993;680-692.
    • (1993) J. Mol. Biol. , vol.232 , pp. 680-692
    • Montgomery, D.1    Jordan, R.2    McMacken, R.3    Freire, E.4
  • 42
    • 0026649409 scopus 로고
    • The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
    • Nelson R. J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E. A. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell. 71:1992;97-105.
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, E.A.5
  • 43
    • 0023809599 scopus 로고
    • +-ATPase activity
    • +-ATPase activity. Methods Enzymol. 156:1988;116-119.
    • (1988) Methods Enzymol. , vol.156 , pp. 116-119
    • Norby, J.G.1
  • 44
    • 0030945296 scopus 로고    scopus 로고
    • GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism
    • Packschies L., Theyssen H., Buchberger A., Bukau B., Goody R. S., Reinstein J. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry. 36:1997;3417-3422.
    • (1997) Biochemistry , vol.36 , pp. 3417-3422
    • Packschies, L.1    Theyssen, H.2    Buchberger, A.3    Bukau, B.4    Goody, R.S.5    Reinstein, J.6
  • 45
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • Palleros D. R., Welch W. J., Fink A. L. Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc. Natl Acad. Sci. USA. 88:1991;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
  • 47
    • 0022969885 scopus 로고
    • Speculations on the functions of the major heat shock and glucose-regulated proteins
    • Pelham H. R. B. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell. 46:1986;959-961.
    • (1986) Cell , vol.46 , pp. 959-961
    • Pelham, H.R.B.1
  • 48
    • 0020348367 scopus 로고
    • Stability of proteins: Proteins which do not present a single cooperative system
    • Privalov P. L. Stability of proteins: proteins which do not present a single cooperative system. Advan. Protein Chem. 35:1982;1-104.
    • (1982) Advan. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 51
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rüdiger J. S., Germeroth L., Schneider-Mergener J., Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16:1997b;1501-1507.
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rüdiger, J.S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 52
    • 0026799491 scopus 로고
    • Unfolded proteins stimulate molecular chaperone hsc70 ATPase by accelerating ADP/ATP exchange
    • Sadis S., Hightower L. E. Unfolded proteins stimulate molecular chaperone hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry. 31:1992;9406-9412.
    • (1992) Biochemistry , vol.31 , pp. 9406-9412
    • Sadis, S.1    Hightower, L.E.2
  • 54
  • 55
    • 0028929052 scopus 로고
    • The DnaK chaperone system of Escherichia coli: Quaternary structures and interactions of the DnaK and GrpE components
    • Schönfeld H.-J., Schmidt D., Schröder H., Bukau B. The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components. J. Biol. Chem. 270:1995;2183-2189.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2183-2189
    • Schönfeld, H.-J.1    Schmidt, D.2    Schröder, H.3    Bukau, B.4
  • 56
    • 0027427986 scopus 로고
    • DnaK, DnaJ, and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder H., Langer T., Hartl F.-U., Bukau B. DnaK, DnaJ, and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12:1993;4137-4144.
    • (1993) EMBO J. , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.-U.3    Bukau, B.4
  • 57
    • 0024226522 scopus 로고
    • Escherichia coli heat shock gene mutants are defective in proteolysis
    • Straus D. B., Walter W. A., Gross C. A. Escherichia coli heat shock gene mutants are defective in proteolysis. Genes Dev. 2:1988;1851-1858.
    • (1988) Genes Dev. , vol.2 , pp. 1851-1858
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 58
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE
    • Szabo A., Langer T., Schröder H., Flanagan J., Bukau B., Hartl F.-U. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE. Proc. Natl Acad. Sci. USA. 91:1994;10345-10349.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schröder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.-U.6
  • 59
    • 0018789686 scopus 로고
    • Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1
    • Takashi R. Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1. Biochemistry. 18:1979;5164-5169.
    • (1979) Biochemistry , vol.18 , pp. 5164-5169
    • Takashi, R.1
  • 61
    • 0020827719 scopus 로고
    • The dnaK protein modulates the heat-shock response of Escherichia coli
    • Tilly K., McKittrick N., Zylicz M., Georgopoulos C. The dnaK protein modulates the heat-shock response of Escherichia coli. Cell. 34:1983;641-646.
    • (1983) Cell , vol.34 , pp. 641-646
    • Tilly, K.1    McKittrick, N.2    Zylicz, M.3    Georgopoulos, C.4
  • 62
    • 0032474433 scopus 로고    scopus 로고
    • NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: A preview of chaperone-protein interaction
    • Wang H., Kurochkin A. V., Pang Y., Hu W., Flynn G. C., Zuiderweg E. R. P. NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction. Biochemistry. 37:1998;7929-7940.
    • (1998) Biochemistry , vol.37 , pp. 7929-7940
    • Wang, H.1    Kurochkin, A.V.2    Pang, Y.3    Hu, W.4    Flynn, G.C.5    Zuiderweg, E.R.P.6
  • 63
    • 0027433805 scopus 로고
    • Identification of the peptide binding domain of hsc70
    • Wang T.-F., Chang J., Wang C. Identification of the peptide binding domain of hsc70. J. Biol. Chem. 268:1993;26049-26051.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26049-26051
    • Wang, T.-F.1    Chang, J.2    Wang, C.3
  • 64
    • 0029101833 scopus 로고
    • ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates
    • Wawrzynów A., Banecki B., Wall D., Liberek K., Georgopoulos C., Zylicz M. ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates. J. Biol. Chem. 270:1995;19307-19311.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19307-19311
    • Wawrzynów, A.1    Banecki, B.2    Wall, D.3    Liberek, K.4    Georgopoulos, C.5    Zylicz, M.6
  • 65
    • 0026684855 scopus 로고
    • Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis
    • Wild J., Kamath-Loeb A., Ziegelhoffer E., Lonetto M., Kawasaki Y., Gross C. A. Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis. Proc. Natl Acad. Sci. USA. 89:1992;7139-7143.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7139-7143
    • Wild, J.1    Kamath-Loeb, A.2    Ziegelhoffer, E.3    Lonetto, M.4    Kawasaki, Y.5    Gross, C.A.6
  • 66
    • 0029814688 scopus 로고    scopus 로고
    • Structure-function analysis of the Escherichia coli GrpE heat shock protein
    • Wu B., Wawrzynów A., Zylicz M., Georgopoulos C. Structure-function analysis of the Escherichia coli GrpE heat shock protein. EMBO J. 15:1996;4806-4816.
    • (1996) EMBO J. , vol.15 , pp. 4806-4816
    • Wu, B.1    Wawrzynów, A.2    Zylicz, M.3    Georgopoulos, C.4
  • 68
    • 0024316732 scopus 로고
    • Initiation of λ DNA replication with purified host- And bacteriophage-encoded proteins: The role of dnaK, dnaJ and grpE heat shock proteins
    • Zylicz M., Ang D., Liberek K., Georgopoulos C. Initiation of λ DNA replication with purified host- and bacteriophage-encoded proteins: the role of dnaK, dnaJ and grpE heat shock proteins. EMBO J. 8:1989;1601-1608.
    • (1989) EMBO J. , vol.8 , pp. 1601-1608
    • Zylicz, M.1    Ang, D.2    Liberek, K.3    Georgopoulos, C.4


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