메뉴 건너뛰기




Volumn 258, Issue 1, 1996, Pages 74-87

Dynamics of the GroEL-Protein complex: Effects of nucleotides and folding mutants

Author keywords

Chaperonin; GroEL; Kinetic analysis; Maltose binding protein; Protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; MALTOSE BINDING PROTEIN; MUTANT PROTEIN;

EID: 0029975103     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0235     Document Type: Article
Times cited : (64)

References (50)
  • 1
    • 0020740241 scopus 로고
    • Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM - A flexible, portable system
    • Barshop, B. A., Wrenn, R. F. & Frieden, C. (1983). Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM - a flexible, portable system. Anal. Biochem. 133, 134-145.
    • (1983) Anal. Biochem. , vol.133 , pp. 134-145
    • Barshop, B.A.1    Wrenn, R.F.2    Frieden, C.3
  • 4
    • 0028027055 scopus 로고
    • Location of a folding protein and shape changes in GroEL-ES complexes imaged by cryoelectron microscopy
    • Chen, S., Roseman, A. M., Hunter, A. S., Wood, S. P., Burston, S. G., Ranson, N. A., Clarke, A. R. & Saibil, H. R. (1994). Location of a folding protein and shape changes in GroEL-ES complexes imaged by cryoelectron microscopy Nature, 371, 261-264.
    • (1994) Nature , vol.371 , pp. 261-264
    • Chen, S.1    Roseman, A.M.2    Hunter, A.S.3    Wood, S.P.4    Burston, S.G.5    Ranson, N.A.6    Clarke, A.R.7    Saibil, H.R.8
  • 6
    • 0024294402 scopus 로고
    • The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein
    • Collier, D. N., Bankaitis, V. A., Weiss, J. B. & Bassford, P. J., Jr (1988). The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein. Cell, 53, 273-283.
    • (1988) Cell , vol.53 , pp. 273-283
    • Collier, D.N.1    Bankaitis, V.A.2    Weiss, J.B.3    Bassford P.J., Jr.4
  • 7
    • 0029019467 scopus 로고
    • The folding of GroEL-bound barnase as a model for chaperonin-mediated refolding
    • Corrales, F. J. & Fersht, A. R. (1995). The folding of GroEL-bound barnase as a model for chaperonin-mediated refolding. Proc. Natl Acad. Sci. USA, 92, 5326-5330.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5326-5330
    • Corrales, F.J.1    Fersht, A.R.2
  • 8
    • 0024554107 scopus 로고
    • The GroES and GroEL heat shock gene products are essential for bacterial growth at all temperatures
    • Fayet, O., Ziegelhoffer, T. & Georgopoulos, C. (1989). The GroES and GroEL heat shock gene products are essential for bacterial growth at all temperatures. J. Bacteriol. 171, 1379-1385.
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 9
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton, W. A., Kashi, Y., Furtak, K. & Horwich, A. L. (1994). Residues in chaperonin GroEL required for polypeptide binding and release. Nature, 371, 614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 10
    • 0028242347 scopus 로고
    • The effect of GroES on the GroEL-dependent assembly of dodecameric glutamine synthetase in the presence of ATP and ADP
    • Fisher, M. T. (1994). The effect of GroES on the GroEL-dependent assembly of dodecameric glutamine synthetase in the presence of ATP and ADP. J. Biol. Chem. 269, 13629-13636.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13629-13636
    • Fisher, M.T.1
  • 12
    • 0026025966 scopus 로고
    • A kinetic partitioning model of selective binding of normative proteins by the bacterial chaperone SecB
    • Hardy J. S. & Randall, L. L. (1991). A kinetic partitioning model of selective binding of normative proteins by the bacterial chaperone SecB. Science, 251, 439-443.
    • (1991) Science , vol.251 , pp. 439-443
    • Hardy, J.S.1    Randall, L.L.2
  • 13
    • 0027925680 scopus 로고
    • Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export
    • Hardy, S. J. S. & Randall, L. L. (1993). Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export. Phil. Trans. Roy. Soc. London. 339, 343-354.
    • (1993) Phil. Trans. Roy. Soc. London. , vol.339 , pp. 343-354
    • Hardy, S.J.S.1    Randall, L.L.2
  • 14
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick, J. P. & Hartl, F. U. (1993). Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 15
    • 0029127242 scopus 로고
    • Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin mediated protein folding
    • Hlodan, R., Tempst, P. & Hartl, F. U. (1995). Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin mediated protein folding. Nature Stuct. Biol. 7, 587-595.
    • (1995) Nature Stuct. Biol. , vol.7 , pp. 587-595
    • Hlodan, R.1    Tempst, P.2    Hartl, F.U.3
  • 16
    • 0028899753 scopus 로고
    • Hydrophobic surfaces that are hidden in chaperonin cpn60 can be exposed by formation of assembly-competent monomers or by ionic perturbation of the oligomer
    • Horowitz, P. M., Hua, S. & Gibbons, D. L. (1995). Hydrophobic surfaces that are hidden in chaperonin cpn60 can be exposed by formation of assembly-competent monomers or by ionic perturbation of the oligomer. J. Biol. Chem. 270, 1535-1542.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1535-1542
    • Horowitz, P.M.1    Hua, S.2    Gibbons, D.L.3
  • 17
    • 0027419011 scopus 로고
    • Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
    • Jackson, G. S., Staniforth, R. A., Halsall, D. J., Atkinson, T., Holbrook, J. J., Clarke, A. & Burston, S. G. (1993). Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry, 32, 2554-2563.
    • (1993) Biochemistry , vol.32 , pp. 2554-2563
    • Jackson, G.S.1    Staniforth, R.A.2    Halsall, D.J.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.6    Burston, S.G.7
  • 18
    • 0027409085 scopus 로고
    • Role of accessory proteins in protein folding
    • Jaenicke, R. (1993). Role of accessory proteins in protein folding. Curr. Opin. Struct. Biol. 3, 104-112.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 104-112
    • Jaenicke, R.1
  • 19
    • 0028583118 scopus 로고
    • Recombinant proteins can be isolated from Escherichia coli cells by repeated cycles of freezing and thawing
    • Johnson, B. H. & Hecht, M. H. (1994). Recombinant proteins can be isolated from Escherichia coli cells by repeated cycles of freezing and thawing. Bio/Technology, 12, 1357-1360.
    • (1994) Bio/Technology , vol.12 , pp. 1357-1360
    • Johnson, B.H.1    Hecht, M.H.2
  • 20
    • 0027182927 scopus 로고
    • Refolding of yeast enolase in the presence of chaperonin GroE
    • Kubo, T., Mizobata, T. & Kawata, Y. (1993). Refolding of yeast enolase in the presence of chaperonin GroE. J. Biol. Chem. 268, 19346-19351.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19346-19351
    • Kubo, T.1    Mizobata, T.2    Kawata, Y.3
  • 21
    • 0025291463 scopus 로고
    • The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor
    • Laminet, A. A., Ziegelhoffer, T., Georgopoulos, C. & Plückthun, A. (1990). The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor. EMBO J. 9, 2315-2319.
    • (1990) EMBO J. , vol.9 , pp. 2315-2319
    • Laminet, A.A.1    Ziegelhoffer, T.2    Georgopoulos, C.3    Plückthun, A.4
  • 22
    • 0023920225 scopus 로고
    • Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in Escherichia coli by multiple wavelength spectrophotometry
    • Lehrer, R. I., Barton, A. & Ganz, T. (1988). Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in Escherichia coli by multiple wavelength spectrophotometry. J. Immunol. Methods, 108, 153-158.
    • (1988) J. Immunol. Methods , vol.108 , pp. 153-158
    • Lehrer, R.I.1    Barton, A.2    Ganz, T.3
  • 23
    • 0029115482 scopus 로고
    • Interaction of GroEL with a highly structured folding intermediate: Iterative binding cycles do not involve unfolding
    • Lilie, H. & Buchner, J. (1995). Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding. Proc. Natl Acad. Sci. USA, 92, 8100-8104.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8100-8104
    • Lilie, H.1    Buchner, J.2
  • 24
    • 0028838951 scopus 로고
    • The hydrophobic nature of GroEL substrate binding
    • Lin, Z., Schwarz, F. P. & Eisenstein, E. (1995). The hydrophobic nature of GroEL substrate binding. J. Biol. Chem. 270, 1011-1014.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1011-1014
    • Lin, Z.1    Schwarz, F.P.2    Eisenstein, E.3
  • 25
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
    • Martin, J., Mayhew, M., Langer, T. & Hartl, F.-U. (1993a). The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature, 366, 228-233.
    • (1993) Nature , vol.366 , pp. 228-233
    • Martin, J.1    Mayhew, M.2    Langer, T.3    Hartl, F.-U.4
  • 26
    • 0027223571 scopus 로고
    • Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formaton in vivo
    • Martin, J. L., Waksman, G., Bardwell, J. C. A., Beckwith, J. & Kuriyan, J. (1993b). Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formaton in vivo. J. Mol. Biol. 230, 1097-1100.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1097-1100
    • Martin, J.L.1    Waksman, G.2    Bardwell, J.C.A.3    Beckwith, J.4    Kuriyan, J.5
  • 27
    • 0025820393 scopus 로고
    • Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanase
    • Mendoza, J. A., Rogers, E., Lorimer, G. H. & Horowitz, P. M. (1991). Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanase. J. Biol. Chem. 266, 13044-13049.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13044-13049
    • Mendoza, J.A.1    Rogers, E.2    Lorimer, G.H.3    Horowitz, P.M.4
  • 28
    • 0026640258 scopus 로고
    • Effects of chaperonin GroE on the refolding of tryptophanase from Escherichia coli
    • Mizobata, T., Akiyama, Y., Ito, K., Yumoto, N. & Kawata, Y. (1992). Effects of chaperonin GroE on the refolding of tryptophanase from Escherichia coli. J. Biol. Chem. 267, 17773-17779.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17773-17779
    • Mizobata, T.1    Akiyama, Y.2    Ito, K.3    Yumoto, N.4    Kawata, Y.5
  • 29
    • 0027112289 scopus 로고
    • 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli
    • Mowbray S. L. & Cole, L. B. (1992). 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli. J. Mol. Biol. 225, 155-175.
    • (1992) J. Mol. Biol. , vol.225 , pp. 155-175
    • Mowbray, S.L.1    Cole, L.B.2
  • 30
    • 0028831186 scopus 로고
    • High selectivity with low specificity: How SecB has solved the paradox of chaperone binding
    • Randall, L. L. & Hardy, S. J. (1995). High selectivity with low specificity: how SecB has solved the paradox of chaperone binding. Trends Biochem. Sci. 20, 65-69.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 65-69
    • Randall, L.L.1    Hardy, S.J.2
  • 31
    • 0027068117 scopus 로고
    • Theory of chaperonin action: Inertial model for enhancement of prokariotic Rubisco assembly
    • Roy, H., Kupferschmid, M. & Bell, A. J. (1992). Theory of chaperonin action: inertial model for enhancement of prokariotic Rubisco assembly Protein Sci. 1, 925-934.
    • (1992) Protein Sci. , vol.1 , pp. 925-934
    • Roy, H.1    Kupferschmid, M.2    Bell, A.J.3
  • 34
    • 0026801563 scopus 로고
    • Interaction of GroE with an all-β-protein
    • Schmidt, M. & Buchner, J. (1992). Interaction of GroE with an all-β-protein. J. Biol. Chem. 267, 16829-16833.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16829-16833
    • Schmidt, M.1    Buchner, J.2
  • 35
    • 0027968020 scopus 로고
    • Correlation between the stability of GroEL-protein ligand complex and the release mechanism
    • Schmidt, M., Bücheler, U., Kaluza, B. & Buchner, J. (1994a). Correlation between the stability of GroEL-protein ligand complex and the release mechanism. J. Biol. Chem. 45, 27964-27972.
    • (1994) J. Biol. Chem. , vol.45 , pp. 27964-27972
    • Schmidt, M.1    Bücheler, U.2    Kaluza, B.3    Buchner, J.4
  • 37
    • 0025754301 scopus 로고
    • The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G.-Y. & Quiocho, F. A. (1991). The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266, 5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3
  • 38
    • 0028231826 scopus 로고
    • Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10
    • Staniforth, R. A., Burston, S. G., Atkinson, T. & Clarke, A. R. (1994). Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10. Biochem. J. 300, 651-658.
    • (1994) Biochem. J. , vol.300 , pp. 651-658
    • Staniforth, R.A.1    Burston, S.G.2    Atkinson, T.3    Clarke, A.R.4
  • 39
    • 0013800421 scopus 로고
    • The interaction of naphtalene dye with apomyoglobin and apohemoglobin. a fluorescent probe of non-polar binding sites
    • Stryer, L. (1965). The interaction of naphtalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13, 482-495.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 41
    • 0025950947 scopus 로고
    • Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli
    • Teschke, C. M., Kim, J., Song, T., Park, S. & Randall, L. L. (1991). Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli. J. Biol. Chem. 266, 11789-11796.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11789-11796
    • Teschke, C.M.1    Kim, J.2    Song, T.3    Park, S.4    Randall, L.L.5
  • 42
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd, J. M., Viitanen, P. V. & Lorimer, G. H. (1994). Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science, 265, 659-666.
    • (1994) Science , vol.265 , pp. 659-666
    • Todd, J.M.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 43
    • 0025940841 scopus 로고
    • Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
    • Viitanen, P. V., Donaldson, G. K., Lorimer, G. H., Lubben, T. H. & Gatenby A. A. (1991). Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry, 30, 9716-9723.
    • (1991) Biochemistry , vol.30 , pp. 9716-9723
    • Viitanen, P.V.1    Donaldson, G.K.2    Lorimer, G.H.3    Lubben, T.H.4    Gatenby, A.A.5
  • 44
    • 0027065105 scopus 로고
    • Purified chaperonin (GroEL) interacts with the normative state of a multitude of Escherichia coli proteins
    • Viitanen, P. V., Gatenby, A. A. & Lorimer, G. H. (1992). Purified chaperonin (GroEL) interacts with the normative state of a multitude of Escherichia coli proteins. Protein Sci. 1, 363-369.
    • (1992) Protein Sci. , vol.1 , pp. 363-369
    • Viitanen, P.V.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 45
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of non-native forms
    • Weissman, J. S., Kashi, Y., Fenton, W. A. & Horwich, A. L. (1994). GroEL-mediated protein folding proceeds by multiple rounds of binding and release of non-native forms. Cell, 78, 693-702.
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.S.1    Kashi, Y.2    Fenton, W.A.3    Horwich, A.L.4
  • 46
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity in the oligomeric chaperonin GroEL
    • Yifrach, O. & Horovitz, A. (1995). Nested cooperativity in the ATPase activity in the oligomeric chaperonin GroEL. Biochemistry, 34, 5303-5308.
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horovitz, A.2
  • 47
    • 0026689459 scopus 로고
    • GroE prevents accumulation of early folding intermediates of pre-β-lactamase without changing the folding pathway
    • Zahn, R. & Plückthun, A. (1992). GroE prevents accumulation of early folding intermediates of pre-β-lactamase without changing the folding pathway. Biochemistry, 31, 3249-3255.
    • (1992) Biochemistry , vol.31 , pp. 3249-3255
    • Zahn, R.1    Plückthun, A.2
  • 48
    • 0028025404 scopus 로고
    • Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature β-lactamase
    • Zahn, R. & Plückthun, A. (1994). Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature β-lactamase. J. Mol. Biol. 242, 165-174.
    • (1994) J. Mol. Biol. , vol.242 , pp. 165-174
    • Zahn, R.1    Plückthun, A.2
  • 49
    • 0028075011 scopus 로고
    • Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequence of β-lactamase precursor
    • Zahn, R., Axmann, S. E., Rücknagel, K.-P., Jaeger, E., Laminet, A. A. & Plückthun, A. (1994). Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequence of β-lactamase precursor. J. Mol. Biol. 242, 150-164.
    • (1994) J. Mol. Biol. , vol.242 , pp. 150-164
    • Zahn, R.1    Axmann, S.E.2    Rücknagel, K.-P.3    Jaeger, E.4    Laminet, A.A.5    Plückthun, A.6
  • 50
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation
    • Zettlmeissl, G., Rudolph, R. & Jaenicke, R. (1979). Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry, 18, 5567-5571.
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.