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Volumn 21, Issue 2, 1996, Pages 179-190

Characterization of the 90 kDa heat shock protein (HSP90)-associated ATP/GTPase

Author keywords

HSP10; HSP27; Methylfluorescein phosphate; Molecular chaperone; Molybdate; Vanadate

Indexed keywords


EID: 0010527137     PISSN: 02505991     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf02703107     Document Type: Article
Times cited : (23)

References (51)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford M M 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding; Anal. Biochem. 72 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0015987426 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet and random coil regions calculated from proteins
    • Chou P Y and Fasman G D 1974 Conformational parameters for amino acids in helical, beta-sheet and random coil regions calculated from proteins; Biochemistry 13 222-245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 4
    • 0023007393 scopus 로고
    • The dynamic state of heat shock proteins in chicken embryo fibroblasts
    • Collier N C and Schlessinger M J 1986 The dynamic state of heat shock proteins in chicken embryo fibroblasts; J. Cell Biol 103 1495-1507
    • (1986) J. Cell Biol , vol.103 , pp. 1495-1507
    • Collier, N.C.1    Schlessinger, M.J.2
  • 5
    • 0025729541 scopus 로고
    • The 90 kDa heat shock protein (HSP90) possesses an ATP-binding site and autophosphorylating activity
    • Csermely P and Kahn C R 1991 The 90 kDa heat shock protein (HSP90) possesses an ATP-binding site and autophosphorylating activity; J. Biol. Chem. 266 4943-4950
    • (1991) J. Biol. Chem. , vol.266 , pp. 4943-4950
    • Csermely, P.1    Kahn, C.R.2
  • 8
    • 0023064835 scopus 로고
    • Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals
    • Dingwall C, Dilworth S M, Black S J, Kearsey S E, Cox L S and Laskey R A 1987 Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals; EMBO J. 6 69-74
    • (1987) EMBO J. , vol.6 , pp. 69-74
    • Dingwall, C.1    Dilworth, S.M.2    Black, S.J.3    Kearsey, S.E.4    Cox, L.S.5    Laskey, R.A.6
  • 9
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus?
    • Dingwall C and Laskey R A 1991 Nuclear targeting sequences - a consensus?; Trends Biochem. Sci. 16 478-481
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 10
    • 0021355126 scopus 로고
    • Complete sequence of the heat shock-inducible HSP90 gene of Saccharomices cerevisiae
    • Farrelly F W and Finkelstein D B 1984 Complete sequence of the heat shock-inducible HSP90 gene of Saccharomices cerevisiae; J. Biol. Chem. 259 5745-5751
    • (1984) J. Biol. Chem. , vol.259 , pp. 5745-5751
    • Farrelly, F.W.1    Finkelstein, D.B.2
  • 11
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Gamier J, Osguthorpe D J and Robson B 1978 Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins; J. Mol. Biol. 120 97-120
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Gamier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 12
    • 0025171925 scopus 로고
    • Nuclear localization of two steroid receptor-associated proteins, HSP90 and p59
    • Gasc J, Renoir J, Faber L E, Delahaye F and Baulieu E 1990 Nuclear localization of two steroid receptor-associated proteins, HSP90 and p59; Exp. Cell Res. 186 362-367
    • (1990) Exp. Cell Res. , vol.186 , pp. 362-367
    • Gasc, J.1    Renoir, J.2    Faber, L.E.3    Delahaye, F.4    Baulieu, E.5
  • 13
    • 0014309996 scopus 로고
    • An automated fluorometric assay for alkaline phosphatase using 3-O-methylfluorescein phosphate
    • Hill H D, Summer G K and Waters M D 1968 An automated fluorometric assay for alkaline phosphatase using 3-O-methylfluorescein phosphate; Anal. Biochem. 24 9-17
    • (1968) Anal. Biochem. , vol.24 , pp. 9-17
    • Hill, H.D.1    Summer, G.K.2    Waters, M.D.3
  • 14
    • 0027985678 scopus 로고
    • All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome"
    • Hutchison K A, Dittmar K D and Pratt W B 1994 All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome"; J. Biol. Chem. 269 27894-27899
    • (1994) J. Biol. Chem. , vol.269 , pp. 27894-27899
    • Hutchison, K.A.1    Dittmar, K.D.2    Pratt, W.B.3
  • 15
    • 0026721458 scopus 로고
    • The protein-protein complex between pp60v-src and HSP90 is stabilized by molybdate, vanadate, tungstate and an endogenous cytosolic metal
    • Hutchison K A, Stancato L F, Jove R and Pratt W B 1992 The protein-protein complex between pp60v-src and HSP90 is stabilized by molybdate, vanadate, tungstate and an endogenous cytosolic metal; J. Biol. Chem. 267 13952-13957
    • (1992) J. Biol. Chem. , vol.267 , pp. 13952-13957
    • Hutchison, K.A.1    Stancato, L.F.2    Jove, R.3    Pratt, W.B.4
  • 16
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of HSP90 and small HSPs as molecular chaperones
    • Jakob U and Buchner J 1994 Assisting spontaneity: the role of HSP90 and small HSPs as molecular chaperones; Trends Biochem. Sci. 19 205-211
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 17
    • 0024358172 scopus 로고
    • A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel
    • Kameshita I and Fujisawa H 1989 A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel; Anal. Biochem. 183 139-143
    • (1989) Anal. Biochem. , vol.183 , pp. 139-143
    • Kameshita, I.1    Fujisawa, H.2
  • 18
    • 0026077464 scopus 로고
    • Characterization and purification of the 94-kDa glucose-regulated protein
    • Kang H S and Welch W J 1991 Characterization and purification of the 94-kDa glucose-regulated protein; J. Biol. Chem. 266 5643-5649
    • (1991) J. Biol. Chem. , vol.266 , pp. 5643-5649
    • Kang, H.S.1    Welch, W.J.2
  • 19
    • 0028156864 scopus 로고
    • In vivo functional protein-protein interaction: Nuclear targeted HSP90 shifts cytoplasmic steroid receptor mutants into the nucleus
    • Kang K I, Devin J, Cadepond F, Jibard N, Guiochon-Mantel A, Baulieu E and Catelli M 1994 In vivo functional protein-protein interaction: nuclear targeted HSP90 shifts cytoplasmic steroid receptor mutants into the nucleus; Proc. Natl. Acad. Sci. U S A 91 340-344
    • (1994) Proc. Natl. Acad. Sci. U S A , vol.91 , pp. 340-344
    • Kang, K.I.1    Devin, J.2    Cadepond, F.3    Jibard, N.4    Guiochon-Mantel, A.5    Baulieu, E.6    Catelli, M.7
  • 20
    • 0029015872 scopus 로고
    • ATP induces dissociation of the 90kDa heat shock protein (HSP90) from F-actin: Interference with the binding of heavy meromyosin
    • Kellermayer MSZ and Csermely P 1995 ATP induces dissociation of the 90kDa heat shock protein (HSP90) from F-actin: interference with the binding of heavy meromyosin; Biochem. Biophys. Res. Commun. 211 166-174
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 166-174
    • Kellermayer, M.S.Z.1    Csermely, P.2
  • 21
    • 0023471689 scopus 로고
    • Calcium coordination and the calmodulin fold: Divergent versus convergent evolution
    • Kretsinger R H 1987 Calcium coordination and the calmodulin fold: divergent versus convergent evolution; Cold Spring Harbor Symp. Quant. Biol. 52 499-510
    • (1987) Cold Spring Harbor Symp. Quant. Biol. , vol.52 , pp. 499-510
    • Kretsinger, R.H.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U K 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4; Nature (London) 227 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0026749007 scopus 로고
    • HSP90 binds specifically to a peptide derived from the highly conserved domain (I) region of p53
    • Lam K T and Calderwood S K 1992 HSP90 binds specifically to a peptide derived from the highly conserved domain (I) region of p53; Biochem. Biophys. Res. Commun. 184 167-174
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 167-174
    • Lam, K.T.1    Calderwood, S.K.2
  • 24
    • 0024548919 scopus 로고
    • Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II
    • Lees-Miller S P and Anderson C W 1989 Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II; J. Biol. Chem. 264 2431-2437
    • (1989) J. Biol. Chem. , vol.264 , pp. 2431-2437
    • Lees-Miller, S.P.1    Anderson, C.W.2
  • 25
    • 0027416853 scopus 로고
    • Bidirectional transport of glucocorticoid receptors across the nuclear envelope
    • Madan P M and DeFranco D B 1993 Bidirectional transport of glucocorticoid receptors across the nuclear envelope; Proc. Natl. Acad. Sci. U S A 90 3588-3592
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , pp. 3588-3592
    • Madan, P.M.1    DeFranco, D.B.2
  • 26
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroEL in chaperonin-assisted protein folding
    • Martin J, Mayhew M, Langer T and Hartl F U 1993 The reaction cycle of GroEL and GroEL in chaperonin-assisted protein folding; Nature (London) 366 228-233
    • (1993) Nature (London) , vol.366 , pp. 228-233
    • Martin, J.1    Mayhew, M.2    Langer, T.3    Hartl, F.U.4
  • 27
    • 0027214861 scopus 로고
    • The calmodulin-binding domain of the mouse 90-kDa heat shock protein
    • Minami Y, Kawasaki H, Suzuki K and Yahara I 1993 The calmodulin-binding domain of the mouse 90-kDa heat shock protein; J. Biol Chem. 268 9604-9610
    • (1993) J. Biol Chem. , vol.268 , pp. 9604-9610
    • Minami, Y.1    Kawasaki, H.2    Suzuki, K.3    Yahara, I.4
  • 28
    • 0028012587 scopus 로고
    • The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo
    • Minami Y, Kimura Y, Kawasaki H, Suzuki K and Yahara I 1994 The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo; Mol. Cell. Biol 14 1459-1464
    • (1994) Mol. Cell. Biol , vol.14 , pp. 1459-1464
    • Minami, Y.1    Kimura, Y.2    Kawasaki, H.3    Suzuki, K.4    Yahara, I.5
  • 29
    • 0025778706 scopus 로고
    • Cytoplasmic 8 S glucocorticoid receptor binds to actin filaments through the 90-kDa heat shock protein moiety
    • Miyata Y and Yahara I 1991 Cytoplasmic 8 S glucocorticoid receptor binds to actin filaments through the 90-kDa heat shock protein moiety; J. Biol Chem. 266 8779-8783
    • (1991) J. Biol Chem. , vol.266 , pp. 8779-8783
    • Miyata, Y.1    Yahara, I.2
  • 30
    • 0026669310 scopus 로고
    • The 90 kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
    • Miyata Y and Yahara I 1992 The 90 kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity; J. Biol. Chem. 267 7042-7047
    • (1992) J. Biol. Chem. , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 31
    • 0029063877 scopus 로고
    • Interaction between casein kinase II and the 90-kDa stress protein, HSP90
    • Miyata Y and Yahara I 1995 Interaction between casein kinase II and the 90-kDa stress protein, HSP90; Biochemistry 34 8123-8129
    • (1995) Biochemistry , vol.34 , pp. 8123-8129
    • Miyata, Y.1    Yahara, I.2
  • 32
    • 0024542186 scopus 로고
    • Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome assignments, and evolutionary origin
    • Moore S K, Kozak C, Robinson E-A, Ullrich S J and Appella E 1989 Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome assignments, and evolutionary origin; J. Biol. Chem. 264 5343-5351
    • (1989) J. Biol. Chem. , vol.264 , pp. 5343-5351
    • Moore, S.K.1    Kozak, C.2    Robinson, E.-A.3    Ullrich, S.J.4    Appella, E.5
  • 33
    • 0027503932 scopus 로고
    • HSP90 associates with specific heat shock puffs (hsr omega) in polytene chromosomes of Drosophila and Chironomus
    • Morcillo G, Diez J L, Carbajal M E and Tanguary R M 1993 HSP90 associates with specific heat shock puffs (hsr omega) in polytene chromosomes of Drosophila and Chironomus; Chromosoma 102 648-659
    • (1993) Chromosoma , vol.102 , pp. 648-659
    • Morcillo, G.1    Diez, J.L.2    Carbajal, M.E.3    Tanguary, R.M.4
  • 34
    • 0027475243 scopus 로고
    • Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl-prolyl isomerases
    • Nadeau K, Das A and Walsh C T 1993 Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl-prolyl isomerases; J. Biol. Chem. 268 1479-1487
    • (1993) J. Biol. Chem. , vol.268 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.T.3
  • 35
    • 0027055047 scopus 로고
    • 83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases
    • Nadeau K, Sullivan M A, Bradley M, Engman D M and Walsh C T 1992 83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases; J. Prot. Sci. 1 970-976
    • (1992) J. Prot. Sci. , vol.1 , pp. 970-976
    • Nadeau, K.1    Sullivan, M.A.2    Bradley, M.3    Engman, D.M.4    Walsh, C.T.5
  • 36
    • 0028230782 scopus 로고
    • Quantitation of the interaction of the immunosuppressant deoxyspergualin and analogs with hsc70 and HSP90
    • Nadeau K, Nadler S G, Saulnier M, Tepper M A and Walsh C T 1994 Quantitation of the interaction of the immunosuppressant deoxyspergualin and analogs with hsc70 and HSP90; Biochemistry 33 2561-2567
    • (1994) Biochemistry , vol.33 , pp. 2561-2567
    • Nadeau, K.1    Nadler, S.G.2    Saulnier, M.3    Tepper, M.A.4    Walsh, C.T.5
  • 37
    • 0029037110 scopus 로고
    • Mutational analysis of HSP90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan D F and Lindquist S 1995 Mutational analysis of HSP90 function: interactions with a steroid receptor and a protein kinase; Mol Cell. Biol. 15 3917-3925
    • (1995) Mol Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 39
    • 33646830005 scopus 로고
    • Ion motive ATPases. I. Ubiquity, properties, and significance to cell function
    • Pedersen P L and Carafoli E 1987 Ion motive ATPases. I. Ubiquity, properties, and significance to cell function; Trends Biochem. Sci. 12 146-150
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 146-150
    • Pedersen, P.L.1    Carafoli, E.2
  • 40
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt W B 1993 The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor; J. Biol. Chem. 268 21455-21458
    • (1993) J. Biol. Chem. , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 41
    • 0028291932 scopus 로고
    • KEKE motifs. Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors
    • Realini C, Rogers S W and Rechsteiner M 1994 KEKE motifs. Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors; FEBS Lett. 348 109-113
    • (1994) FEBS Lett. , vol.348 , pp. 109-113
    • Realini, C.1    Rogers, S.W.2    Rechsteiner, M.3
  • 42
    • 0027203053 scopus 로고
    • Kinetic control of Ca(II) signaling: Tuning the ion dissociation rates of EF-hand Ca(II) binding sites
    • Renner M, Danielson M A and Falke J J 1993 Kinetic control of Ca(II) signaling: tuning the ion dissociation rates of EF-hand Ca(II) binding sites; Proc. Natl. Acad. Sci. U S A 90 6493-6497
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , pp. 6493-6497
    • Renner, M.1    Danielson, M.A.2    Falke, J.J.3
  • 43
    • 0028157317 scopus 로고
    • Isolation of a cDNA clone specifying rat chaperonin 10, a stress-inducible mitochondrial matrix protein synthesized without a cleavable presequence
    • Ryan M T, Hoogenraad N J and Hoj P B 1994 Isolation of a cDNA clone specifying rat chaperonin 10, a stress-inducible mitochondrial matrix protein synthesized without a cleavable presequence; FEBS Lett. 337 152-156
    • (1994) FEBS Lett. , vol.337 , pp. 152-156
    • Ryan, M.T.1    Hoogenraad, N.J.2    Hoj, P.B.3
  • 44
    • 0029094175 scopus 로고
    • Affinity purification, overexpression, and characterization of chaperonin 10 homologues synthesized with and without N-terminal acetylation
    • Ryan M T, Naylor D J, Hoogenraad N J and Hoj P B 1995 Affinity purification, overexpression, and characterization of chaperonin 10 homologues synthesized with and without N-terminal acetylation; J. Biol. Chem. 270 22037-22043
    • (1995) J. Biol. Chem. , vol.270 , pp. 22037-22043
    • Ryan, M.T.1    Naylor, D.J.2    Hoogenraad, N.J.3    Hoj, P.B.4
  • 45
    • 0026553759 scopus 로고
    • Comparison of the 90-kilodalton heat shock protein interaction with in vitro translated glucocorticoid and estrogen receptors
    • Schlatter L K, Howard K J, Parker M G and Distelhorst C W 1992 comparison of the 90-kilodalton heat shock protein interaction with in vitro translated glucocorticoid and estrogen receptors; Mol. Endocrinol. 6 132-140
    • (1992) Mol. Endocrinol. , vol.6 , pp. 132-140
    • Schlatter, L.K.1    Howard, K.J.2    Parker, M.G.3    Distelhorst, C.W.4
  • 46
    • 0021424434 scopus 로고
    • Organic extraction of Pi with isobutanol/toluene
    • Shacter E 1984 Organic extraction of Pi with isobutanol/toluene; Anal. Biochem. 138 416-420
    • (1984) Anal. Biochem. , vol.138 , pp. 416-420
    • Shacter, E.1
  • 47
    • 0028224526 scopus 로고
    • Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and characterization of their interactions
    • Shi Y, Brown E D and Walsh C T 1994 Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and characterization of their interactions; Proc. Natl. Acad. Sci. U S A 91 2767-2771
    • (1994) Proc. Natl. Acad. Sci. U S A , vol.91 , pp. 2767-2771
    • Shi, Y.1    Brown, E.D.2    Walsh, C.T.3
  • 48
    • 0027239861 scopus 로고
    • Mutational analysis of HSP90 binding to the progesterone receptor
    • Sullivan W P and Toft D O 1993 Mutational analysis of HSP90 binding to the progesterone receptor; J. Biol. Chem. 268 20373-20379
    • (1993) J. Biol. Chem. , vol.268 , pp. 20373-20379
    • Sullivan, W.P.1    Toft, D.O.2
  • 50
    • 0027159830 scopus 로고
    • Biochemical and immunological evidence that an acidic domain of HSP90 is involved in the stabilization of untransformed glucocorticoid receptor complexes
    • Tbarka N, Richard-Mereau C, Formstecher P and Dautrevaux M 1993 Biochemical and immunological evidence that an acidic domain of HSP90 is involved in the stabilization of untransformed glucocorticoid receptor complexes; FEBS Lett. 322 125-128
    • (1993) FEBS Lett. , vol.322 , pp. 125-128
    • Tbarka, N.1    Richard-Mereau, C.2    Formstecher, P.3    Dautrevaux, M.4


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