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Volumn 5, Issue 3, 1997, Pages 403-414

Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain

Author keywords

ATPase; calcium binding motif; Hsp70; molecular chaperone

Indexed keywords


EID: 0031569356     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00197-4     Document Type: Article
Times cited : (128)

References (51)
  • 1
    • 0029566336 scopus 로고
    • The role of molecular chaperones in protein folding
    • Hendrick, J.P. & Hartl, F.-U. (1995). The role of molecular chaperones in protein folding. FASEB J. 9, 1559-1569.
    • (1995) FASEB J. , vol.9 , pp. 1559-1569
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 2
    • 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
  • 4
    • 0027493262 scopus 로고
    • Regulation of hsp70 synthesis induced by cupric sulfate and zinc sulfate in thermotolerant HeLa cells
    • Hatayama, T., Asai, Y., Wakatsuki, T., Kitamura, T. & Imahara, H. (1993). Regulation of hsp70 synthesis induced by cupric sulfate and zinc sulfate in thermotolerant HeLa cells. J. Biochem. 114, 592-597.
    • (1993) J. Biochem. , vol.114 , pp. 592-597
    • Hatayama, T.1    Asai, Y.2    Wakatsuki, T.3    Kitamura, T.4    Imahara, H.5
  • 6
    • 0023003446 scopus 로고
    • Calcium ionophore A23187 as a regulator of gene expression in mammalian cells
    • Resendez, E., Jr., Ting, J., Kim, S., Wodden, S.K. & Lee, A.S. (1986). Calcium ionophore A23187 as a regulator of gene expression in mammalian cells. J. Cell. Biol. 103, 2145-2152.
    • (1986) J. Cell. Biol. , vol.103 , pp. 2145-2152
    • Resendez Jr., E.1    Ting, J.2    Kim, S.3    Wodden, S.K.4    Lee, A.S.5
  • 7
    • 0029027434 scopus 로고
    • Structure and regulation of the mouse Grp78 (BiP) promoter by glucose and calcium ionophore
    • Tillman, J.B., Mote, P.L., Walford, R.L. & Spindler, S.R. (1995). Structure and regulation of the mouse Grp78 (BiP) promoter by glucose and calcium ionophore. Gene 158, 225-229.
    • (1995) Gene , vol.158 , pp. 225-229
    • Tillman, J.B.1    Mote, P.L.2    Walford, R.L.3    Spindler, S.R.4
  • 8
    • 0020827719 scopus 로고
    • The DnaK protein modulates the heat-shock response of Escherichia coli
    • Tilly, K., McKittrick, N., Zylicz, M. & Georgopoulos, C. (1983). The DnaK protein modulates the heat-shock response of Escherichia coli. Cell 34, 641-646.
    • (1983) Cell , vol.34 , pp. 641-646
    • Tilly, K.1    McKittrick, N.2    Zylicz, M.3    Georgopoulos, C.4
  • 9
    • 0043104253 scopus 로고
    • The DnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system
    • Zylicz, M., LeBowitz, J.H., McMacken, R. & Georgopoulos, C. (1983). The DnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system. Proc. Natl. Acad. Sci. USA 80, 6431-6435.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6431-6435
    • Zylicz, M.1    LeBowitz, J.H.2    McMacken, R.3    Georgopoulos, C.4
  • 10
    • 0028240468 scopus 로고
    • Structural basis of the 70 kilodalton heat shock cognate protein ATP hydrolytic activity
    • Flaherty, K.M., Wilbanks, S.M., DeLuca-Flaherty, C. & McKay, D.B. (1994). Structural basis of the 70 kilodalton heat shock cognate protein ATP hydrolytic activity J. Biol. Chem. 269, 12899-12907.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12899-12907
    • Flaherty, K.M.1    Wilbanks, S.M.2    DeLuca-Flaherty, C.3    McKay, D.B.4
  • 11
    • 0028938819 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70
    • Wilbanks, S.M. & McKay, D.B. (1995). How potassium affects the activity of the molecular chaperone Hsc70. J. Biol. Chem. 270, 2251-2257.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2251-2257
    • Wilbanks, S.M.1    McKay, D.B.2
  • 12
    • 0026649409 scopus 로고
    • The translation machinery and 70kD heat shock protein cooperate in protein synthesis
    • Nelson, R.J., Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M. & Craig, E.A. (1992). The translation machinery and 70kD heat shock protein cooperate in protein synthesis. Cell 71, 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
  • 13
    • 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. (1990). Interaction of Hsp70 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    Mizzen, L.A.2    Welch, W.J.3
  • 14
    • 0024988094 scopus 로고
    • The E. coli dnaK gene product, the Hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner
    • Skowyra, D., Georgopoulos, C. & Zylicz, M. (1990). The E. coli dnaK gene product, the Hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner. Cell 62, 939-944.
    • (1990) Cell , vol.62 , pp. 939-944
    • Skowyra, D.1    Georgopoulos, C.2    Zylicz, M.3
  • 15
    • 0023052239 scopus 로고
    • An hsp70-like protein in the ER: Identify with the 78 kD glucose-regulated protein and immunoglobulin heavy-chain binding protein
    • Munro, S. & Pelham, H. (1986). An hsp70-like protein in the ER: identify with the 78 kD glucose-regulated protein and immunoglobulin heavy-chain binding protein. Cell 46, 291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.2
  • 16
    • 0024298706 scopus 로고
    • 70 K heat shock related proteins stimulate protein translocation into microsomes
    • Chirico, W.J., Waters, M.G. & Blobel, G. (1988). 70 K heat shock related proteins stimulate protein translocation into microsomes. Nature 332, 805-810.
    • (1988) Nature , vol.332 , pp. 805-810
    • Chirico, W.J.1    Waters, M.G.2    Blobel, G.3
  • 17
    • 0024268186 scopus 로고
    • 70kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria
    • Murakami, H., Pain, D., & Blobel, G. (1988). 70kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria. J. Cell Biol. 107, 2051-2057.
    • (1988) J. Cell Biol. , vol.107 , pp. 2051-2057
    • Murakami, H.1    Pain, D.2    Blobel, G.3
  • 18
    • 0025039149 scopus 로고
    • Requirements for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang, P.-O., Ostermann, J., Shilling, J., Neupert, W., Craig, E.A. & Pfanner, N. (1990). Requirements for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348, 137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.-O.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 19
    • 0026643651 scopus 로고
    • The transport of proteins into the nucleus requires the 70 Kilodalton heat shock protein or its cytosolic cognate
    • Shi, Y. & Thomas J.O. (1992). The transport of proteins into the nucleus requires the 70 Kilodalton heat shock protein or its cytosolic cognate. Mol. Cell. Biol. 12, 2186-2192.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2186-2192
    • Shi, Y.1    Thomas, J.O.2
  • 20
    • 0027946910 scopus 로고
    • Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria
    • Wagner, I., Arlt, H., vanDyck, L., Langer, T. & Neupert W. (1994). Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13, 5135-5145.
    • (1994) EMBO J. , vol.13 , pp. 5135-5145
    • Wagner, I.1    Arlt, H.2    VanDyck, L.3    Langer, T.4    Neupert, W.5
  • 21
    • 0025218811 scopus 로고
    • Self-regulation of 70 kilodalton heat shock proteins in Saccharomyces cerevisiae
    • Stone, D.E. & Craig, E.A. (1990). Self-regulation of 70 kilodalton heat shock proteins in Saccharomyces cerevisiae. Mol. Cell Biol. 10, 1622-1632.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 1622-1632
    • Stone, D.E.1    Craig, E.A.2
  • 22
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abavaya, K., Myers, M.P., Murphy, S.P. & Morimoto, R.I. (1992). The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev. 6, 1153-1164.
    • (1992) Genes Dev. , vol.6 , pp. 1153-1164
    • Abavaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 23
    • 0027194027 scopus 로고
    • The immunoglobulin-binding protein in vitro autophosphorylation site maps to a threonine within the ATP binding cleft but is not a detectable site of in vivo phosphorylation
    • Gaut, J.R. & Hendershot, L.M. (1993). The immunoglobulin-binding protein in vitro autophosphorylation site maps to a threonine within the ATP binding cleft but is not a detectable site of in vivo phosphorylation. J. Biol. Chem. 268, 12691-12696.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12691-12696
    • Gaut, J.R.1    Hendershot, L.M.2
  • 24
    • 0026051442 scopus 로고
    • Calcium-dependent autophosphorylation of the glucose-regulated protein, Grp78
    • Leustek, T., Toledo, H., Brot, N. & Weissbach, H. (1991). Calcium-dependent autophosphorylation of the glucose-regulated protein, Grp78. Arch. Biochem. Biophys. 289, 256-261.
    • (1991) Arch. Biochem. Biophys. , vol.289 , pp. 256-261
    • Leustek, T.1    Toledo, H.2    Brot, N.3    Weissbach, H.4
  • 25
    • 0026076490 scopus 로고
    • DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity
    • McCarty, J.S. & Walker, G.C. (1991). DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc. Nat. Acad. Sci. USA 88, 9513-9517.
    • (1991) Proc. Nat. Acad. Sci. USA , vol.88 , pp. 9513-9517
    • McCarty, J.S.1    Walker, G.C.2
  • 26
    • 0022002022 scopus 로고
    • Structure and expression of the human gene encoding major heat shock protein Hsp70
    • Wu, B., Hunt, C. & Morimoto, R.I. (1985). Structure and expression of the human gene encoding major heat shock protein Hsp70. Mol. Cell. Biol. 5, 330-341.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 330-341
    • Wu, B.1    Hunt, C.2    Morimoto, R.I.3
  • 27
    • 0023649886 scopus 로고
    • Structure and expression of a human gene coding for a 71 kD heat shock 'cognate' protein
    • Dworniczak, B. & Mirault, M.E. (1987). Structure and expression of a human gene coding for a 71 kD heat shock 'cognate' protein. Nucleic Acids Res. 15, 5181-5197.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 5181-5197
    • Dworniczak, B.1    Mirault, M.E.2
  • 28
    • 0028926541 scopus 로고
    • Cloning and subcellular localization of human mitochondrial Hsp70
    • Bhattacharyya, T., et al., & Morimoto, R.I. (1995). Cloning and subcellular localization of human mitochondrial Hsp70. J. Biol. Chem. 270, 1705-1710.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1705-1710
    • Bhattacharyya, T.1    Morimoto, R.I.2
  • 29
    • 0000097632 scopus 로고
    • Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70
    • Hunt, C & Morimoto, R.I. (1985). Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl. Acad. Sci. USA 82, 6455-6459.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6455-6459
    • Hunt, C.1    Morimoto, R.I.2
  • 30
    • 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. (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
  • 31
    • 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. (1996). 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, 2969-2979.
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 32
    • 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., et al., & Bukau, B. (1995). Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem. 270, 16903-16910.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16903-16910
    • Buchberger, A.1    Bukau, B.2
  • 33
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K.M., DeLuca-Flaherty, C. & McKay, D.B. (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
  • 35
    • 0029937037 scopus 로고    scopus 로고
    • Structural analysis of substrate binding by the molecular chaperone DnaK
    • Zhu, X., et al., & Hendrickson, W.A. (1996). Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272, 1606-1614.
    • (1996) Science , vol.272 , pp. 1606-1614
    • Zhu, X.1    Hendrickson, W.A.2
  • 37
    • 0027943510 scopus 로고
    • The crystal structure of the bacterial chaperonin Gro EL at 2.8 Å
    • Braig, K., et al., & Sigler, P.B. (1994). The crystal structure of the bacterial chaperonin Gro EL at 2.8 Å. Nature 371, 578-586.
    • (1994) Nature , vol.371 , pp. 578-586
    • Braig, K.1    Sigler, P.B.2
  • 38
    • 0029664944 scopus 로고    scopus 로고
    • The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP-gamma-S
    • Boisvert, D.C., Wang, J.M., Otwinowski, Z., Horwich, A.L. & Sigler, P.B. (1996). The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP-gamma-S. Nat. Struct. Biol. 3, 170-177.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 170-177
    • Boisvert, D.C.1    Wang, J.M.2    Otwinowski, Z.3    Horwich, A.L.4    Sigler, P.B.5
  • 40
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70 kDa heat shock cognate protein
    • Flaherty, K.M., McKay, D.B., Kabsch, W. & Holmes, K.C. (1991). Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70 kDa heat shock cognate protein. Proc. Nat. Acad. Sci. USA 88, 5041-5045.
    • (1991) Proc. Nat. Acad. Sci. USA , vol.88 , pp. 5041-5045
    • Flaherty, K.M.1    McKay, D.B.2    Kabsch, W.3    Holmes, K.C.4
  • 41
    • 0028382510 scopus 로고
    • A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE
    • Buchberger, A., Schroder, H., Buttner, M., Valencia, A. & Bukau B. (1994). A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat. Struct. Biol. 1, 95-101.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 95-101
    • Buchberger, A.1    Schroder, H.2    Buttner, M.3    Valencia, A.4    Bukau, B.5
  • 42
    • 0029101833 scopus 로고
    • ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates
    • Wawrzynow, A., Banecki, B., Wall, D., Liberek, K. & Georgopoulos, C. (1995). 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, 19307-19311.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19307-19311
    • Wawrzynow, A.1    Banecki, B.2    Wall, D.3    Liberek, K.4    Georgopoulos, C.5
  • 44
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker, J.P. (1990). Structural aspects of metal liganding to functional groups in proteins. Adv. Protein Chem. 42, 1-76.
    • (1990) Adv. Protein Chem. , vol.42 , pp. 1-76
    • Glusker, J.P.1
  • 45
    • 0030018744 scopus 로고    scopus 로고
    • Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis
    • O'Brien, M.C., Flaherty, K.M. & McKay, D.B. (1996). Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis. J. Biol. Chem. 271, 15874-15878.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15874-15878
    • O'Brien, M.C.1    Flaherty, K.M.2    McKay, D.B.3
  • 46
    • 0027484169 scopus 로고
    • Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis
    • O'Brien, M.C. & McKay, D.B. (1993). Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis. J. Biol. Chem. 268, 24323-24329.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24323-24329
    • O'Brien, M.C.1    McKay, D.B.2
  • 47
    • 0028877021 scopus 로고
    • Interaction of calcium with Bordetella pertussis adenylate cyclase toxin
    • Rose, T., Sebo, P., Bellalou, J. & Ladant, D. (1995). Interaction of calcium with Bordetella pertussis adenylate cyclase toxin. J. Biol. Chem. 270, 26370-26376.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26370-26376
    • Rose, T.1    Sebo, P.2    Bellalou, J.3    Ladant, D.4
  • 48
    • 0028950021 scopus 로고
    • Adenylate-cyclase activity from Hirudo medicinalis segmental ganglia: Modulation by calcium and calmodulin
    • Ferretti, M.E. (1995). Adenylate-cyclase activity from Hirudo medicinalis segmental ganglia: modulation by calcium and calmodulin. Comp. Biochem. Physiol. 110, 79-86.
    • (1995) Comp. Biochem. Physiol. , vol.110 , pp. 79-86
    • Ferretti, M.E.1
  • 50
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. & Wilson, K.S. (1993). Automated refinement of protein models. Acta Cryst. D 49, 129-147.
    • (1993) Acta Cryst. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 51
    • 84889120137 scopus 로고
    • Improved methods for building proteins models in electron-density maps and the location of errors in these models
    • Jones, AT., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building proteins models in electron-density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, A.T.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4


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