메뉴 건너뛰기




Volumn 286, Issue 4, 1999, Pages 1241-1249

Conformational changes in the chaperonin GroEL: New insights into the allosteric mechanism

Author keywords

Co operativity; Computer simulation; Essential dynamics; Protein dynamics; X ray crystallography

Indexed keywords

BACTERIAL PROTEIN; CHAPERONIN; NUCLEOTIDE BINDING PROTEIN;

EID: 0033525835     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2568     Document Type: Article
Times cited : (62)

References (58)
  • 2
    • 0029583647 scopus 로고
    • The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer
    • Azem A., Diamant S., Kessel M., Weiss C., Goloubinoff P. The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer. Proc. Natl Acad. Sci. USA. 92:1995;12021-12025.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 12021-12025
    • Azem, A.1    Diamant, S.2    Kessel, M.3    Weiss, C.4    Goloubinoff, P.5
  • 3
    • 0030995661 scopus 로고    scopus 로고
    • Nucleotide-dependent complex formation between the Eschericia coli chaperonins GroEL and GroES studied under equilibrium conditions
    • Behlke J., Ristau O., Schönfeld H.-J. Nucleotide-dependent complex formation between the Eschericia coli chaperonins GroEL and GroES studied under equilibrium conditions. Biochemistry. 36:1997;5149-5156.
    • (1997) Biochemistry , vol.36 , pp. 5149-5156
    • Behlke, J.1    Ristau, O.2    Schönfeld, H.-J.3
  • 4
    • 0030904524 scopus 로고    scopus 로고
    • Novel methods of sampling phase space in the simulation of biological systems
    • Berne B. J., Straub J. E. Novel methods of sampling phase space in the simulation of biological systems. Curr. Opin. Struct. Biol. 7:1997;181-189.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 181-189
    • Berne, B.J.1    Straub, J.E.2
  • 9
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig K., Adams P. D., Brünger A. T. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nature Struct. Biol. 2:1995;1083-1094.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brünger, A.T.3
  • 10
    • 0030966765 scopus 로고    scopus 로고
    • A structural model for GroEL-polypeptide recognition
    • Buckle A. M., Zahn R., Fersht A. R. A structural model for GroEL-polypeptide recognition. Proc. Natl Acad. Sci. USA. 94:1997;3571-3575.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3571-3575
    • Buckle, A.M.1    Zahn, R.2    Fersht, A.R.3
  • 11
  • 12
    • 0028027055 scopus 로고
    • Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
    • Chen S., Roseman A. M., Hunter A. S., Wood S. P., Burston S. G., Ranson N. A., Clarke A. R., Saibil H. R. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature. 371:1994;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
  • 13
    • 0029664316 scopus 로고    scopus 로고
    • Toward a mechanism for GroEL-GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
    • Corrales F. J., Fersht A. R. Toward a mechanism for GroEL-GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Proc. Natl Acad. Sci. USA. 93:1996;4509-4512.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4509-4512
    • Corrales, F.J.1    Fersht, A.R.2
  • 16
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of molscript that includes greatly enhanced coloring capabilities
    • Esnouf R. M. An extensively modified version of molscript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15:1997;132-134, 112-113.
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 17
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton W. A., Horwich A. L. GroEL-mediated protein folding. Protein Sci. 6:1997;743-760.
    • (1997) Protein Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 18
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton W. A., Kasl Y., Furtak K., Horwich A. L. Residues in chaperonin GroEL required for polypeptide binding and release. Nature. 371:1994;614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kasl, Y.2    Furtak, K.3    Horwich, A.L.4
  • 19
    • 0000577041 scopus 로고
    • Large-amplitude nonlinear motions in proteins
    • Garcia A. E. Large-amplitude nonlinear motions in proteins. Phys. Rev. Letters. 68:1992;2696-2699.
    • (1992) Phys. Rev. Letters , vol.68 , pp. 2696-2699
    • Garcia, A.E.1
  • 20
    • 0025995773 scopus 로고
    • Cooperativity in ATP hydrolysis by GroEL is increased by GroES
    • Gray T. E., Fersht A. R. Cooperativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Letters. 292:1991;254-258.
    • (1991) FEBS Letters , vol.292 , pp. 254-258
    • Gray, T.E.1    Fersht, A.R.2
  • 21
    • 0029858706 scopus 로고    scopus 로고
    • Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
    • Hayer-Hartl M. K., Weber F., Hartl F. U. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J. 15:1996;6111-6121.
    • (1996) EMBO J. , vol.15 , pp. 6111-6121
    • Hayer-Hartl, M.K.1    Weber, F.2    Hartl, F.U.3
  • 22
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward S., Berendsen H. J. C. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins: Struct. Funct. Genet. 30:1998;144-154.
    • (1998) Proteins: Struct. Funct. Genet. , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.C.2
  • 23
    • 0030888546 scopus 로고    scopus 로고
    • Model free methods of analyzing domain motions in proteins from simulation: A comparison of normal mode analysis and molecular dynamics simulation of lysozyme
    • Hayward S., Kitao A., Berendsen H. J. C. Model free methods of analyzing domain motions in proteins from simulation: a comparison of normal mode analysis and molecular dynamics simulation of lysozyme. Proteins: Struct. Funct. Genet. 27:1997;425-437.
    • (1997) Proteins: Struct. Funct. Genet. , vol.27 , pp. 425-437
    • Hayward, S.1    Kitao, A.2    Berendsen, H.J.C.3
  • 25
    • 0018791204 scopus 로고
    • Purification and properties of GroE, a host protein involved in bacteriophage assembly
    • Hendrix R. W. Purification and properties of GroE, a host protein involved in bacteriophage assembly. J. Mol. Biol. 129:1979;375-392.
    • (1979) J. Mol. Biol. , vol.129 , pp. 375-392
    • Hendrix, R.W.1
  • 26
    • 0032005913 scopus 로고    scopus 로고
    • Structural aspects of GroEL function
    • Horovitz A. Structural aspects of GroEL function. Curr. Opin. Struct. Biol. 8:1998;93-100.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 93-100
    • Horovitz, A.1
  • 27
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
    • Hunt J. F., Weaver A. J., Landry S., Gierasch L., Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature. 379:1996;37-45.
    • (1996) Nature , vol.379 , pp. 37-45
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.3    Gierasch, L.4    Deisenhofer, J.5
  • 28
    • 0030827121 scopus 로고    scopus 로고
    • GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex
    • Inbar E., Horovitz A. GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex. Biochemistry. 36:1997;12276-12281.
    • (1997) Biochemistry , vol.36 , pp. 12276-12281
    • Inbar, E.1    Horovitz, A.2
  • 29
    • 0026605821 scopus 로고
    • Structure of holo-chaperonin studied with electron-microscopy
    • Ishii N., Taguchi H., Sumi M., Yoshida M. Structure of holo-chaperonin studied with electron-microscopy. FEBS Letters. 299:1992;169-174.
    • (1992) FEBS Letters , vol.299 , pp. 169-174
    • Ishii, N.1    Taguchi, H.2    Sumi, M.3    Yoshida, M.4
  • 30
    • 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. R., Burston S. G. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry. 32:1993;2554-2263.
    • (1993) Biochemistry , vol.32 , pp. 2554-2263
    • Jackson, G.S.1    Staniforth, R.A.2    Halsall, D.J.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.R.6    Burston, S.G.7
  • 31
    • 0032562652 scopus 로고    scopus 로고
    • Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings
    • Kad N. M., Ranson N. A., Cliff M. J., Clarke A. R. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings. J. Mol. Biol. 278:1998;267-278.
    • (1998) J. Mol. Biol. , vol.278 , pp. 267-278
    • Kad, N.M.1    Ranson, N.A.2    Cliff, M.J.3    Clarke, A.R.4
  • 32
    • 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
  • 33
    • 0027092285 scopus 로고
    • Chaperonin-mediated proteinfolding: GroES binds to one end of the GroEL cylinder, which accomodates the protein within its central cavity
    • Langer T., Pfeifer G., Martin J., Baumeister W., Hartl F. U. Chaperonin-mediated proteinfolding: GroES binds to one end of the GroEL cylinder, which accomodates the protein within its central cavity. EMBO J. 11:1992;4757-4765.
    • (1992) EMBO J. , vol.11 , pp. 4757-4765
    • Langer, T.1    Pfeifer, G.2    Martin, J.3    Baumeister, W.4    Hartl, F.U.5
  • 34
    • 0021449809 scopus 로고
    • Quasi-harmonic method for studying very low frequency modes in proteins
    • Levy R. M., Srinivasan A. R., Olson W. K., McCammon J. A. Quasi-harmonic method for studying very low frequency modes in proteins. Biopolymers. 23:1984;1099-1112.
    • (1984) Biopolymers , vol.23 , pp. 1099-1112
    • Levy, R.M.1    Srinivasan, A.R.2    Olson, W.K.3    McCammon, J.A.4
  • 35
    • 0030902005 scopus 로고    scopus 로고
    • Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings
    • Llorca O., Marco S., Carrascosa J., Valpuesta J. Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings. FEBS Letters. 405:1997a;195-199.
    • (1997) FEBS Letters , vol.405 , pp. 195-199
    • Llorca, O.1    Marco, S.2    Carrascosa, J.3    Valpuesta, J.4
  • 36
    • 0031438410 scopus 로고    scopus 로고
    • Effects of inter-ring communication in GroEL structural and functional asymetry
    • Llorca O., Péréz J., Carrascosa J. L., Galán A., Muga A. Effects of inter-ring communication in GroEL structural and functional asymetry. J. Biol. Chem. 272:1997b;32925-32932.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32925-32932
    • Llorca, O.1    Péréz, J.2    Carrascosa, J.L.3    Galán, A.4    Muga, A.5
  • 37
    • 0032555216 scopus 로고    scopus 로고
    • The allosteric mechnism of GroEL: A dynamic analysis
    • Ma J., Karplus M. The allosteric mechnism of GroEL: a dynamic analysis. Proc. Natl Acad. Sci. USA. 95:1998;8502-8507.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8502-8507
    • Ma, J.1    Karplus, M.2
  • 40
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E. A., Bacon D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 41
    • 0029087065 scopus 로고
    • Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds
    • Ranson N. A., Dunster N. J., Burston S. G., Clark A. R. Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. J. Mol. Biol. 250:1995;581-586.
    • (1995) J. Mol. Biol. , vol.250 , pp. 581-586
    • Ranson, N.A.1    Dunster, N.J.2    Burston, S.G.3    Clark, A.R.4
  • 42
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman A. M., Chen S., White H., Braig K., Saibil H. R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 44
    • 0030918284 scopus 로고    scopus 로고
    • Biomolecular dynamics at long time steps: Bridging the timescale gap between simulation and experimentation
    • Schlick T., Barth E., Mandziuk M. Biomolecular dynamics at long time steps: bridging the timescale gap between simulation and experimentation. Annu. Rev. Biomol. Struct. 26:1997;181-222.
    • (1997) Annu. Rev. Biomol. Struct. , vol.26 , pp. 181-222
    • Schlick, T.1    Barth, E.2    Mandziuk, M.3
  • 45
    • 0031037687 scopus 로고    scopus 로고
    • Catalysis of protein folding by symmetric chaperone complexes
    • Sparrer H., Rutkat K., Buchner J. Catalysis of protein folding by symmetric chaperone complexes. Proc. Natl Acad. Sci. USA. 94:1997;1096-1100.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1096-1100
    • Sparrer, H.1    Rutkat, K.2    Buchner, J.3
  • 46
    • 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. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10. Biochem. J. 300:1994;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
  • 47
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd M. J., Viitanen P. V., Lorimer G. H. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science. 265:1994;659-666.
    • (1994) Science , vol.265 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 49
    • 0029586726 scopus 로고
    • Essential dynamics of the cellular retinol binding protein - evidence for ligand induced conformational changes
    • Van Aalten D. M. F., Findlay J. B. C., Amadei A., Berendsen H. J. C. Essential dynamics of the cellular retinol binding protein - evidence for ligand induced conformational changes. Protein Eng. 8:1995b;1129-1136.
    • (1995) Protein Eng. , vol.8 , pp. 1129-1136
    • Van Aalten, D.M.F.1    Findlay, J.B.C.2    Amadei, A.3    Berendsen, H.J.C.4
  • 50
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • Weissman J. S., Kashi Y., Fenton W. A., Horwich A. L. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell. 78:1994;693-702.
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.S.1    Kashi, Y.2    Fenton, W.A.3    Horwich, A.L.4
  • 52
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediate protein folding reaction
    • Weissman J. S., Rye H. S., Fenton W. A., A L., Horwich J. M. B. Characterization of the active intermediate of a GroEL-GroES-mediate protein folding reaction. Cell. 84:1996;481-490.
    • (1996) Cell , vol.84 , pp. 481-490
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    A., L.4    Horwich, J.M.B.5
  • 55
    • 0028135063 scopus 로고
    • Two lines of allosteric communication in the oligomeric chaperoninGroEL are revealed by the single mutation Arg196→Ala
    • Yifrach O., Horovitz A. Two lines of allosteric communication in the oligomeric chaperoninGroEL are revealed by the single mutation Arg196→Ala. J. Mol. Biol. 243:1994;397-401.
    • (1994) J. Mol. Biol. , vol.243 , pp. 397-401
    • Yifrach, O.1    Horovitz, A.2
  • 56
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
    • Yifrach O., Horovitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry. 34:1995;5303-5308.
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horovitz, A.2
  • 57
    • 0029995319 scopus 로고    scopus 로고
    • Allosteric control by ATP of non-folded protein binding to GroEL
    • Yifrach O., Horovitz A. Allosteric control by ATP of non-folded protein binding to GroEL. J. Mol. Biol. 255:1996;356-361.
    • (1996) J. Mol. Biol. , vol.255 , pp. 356-361
    • Yifrach, O.1    Horovitz, A.2
  • 58
    • 0030061845 scopus 로고    scopus 로고
    • Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
    • Zahn R., Perrett S., Stenberg G., Fersht A. R. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science. 271:1996;642-645.
    • (1996) Science , vol.271 , pp. 642-645
    • Zahn, R.1    Perrett, S.2    Stenberg, G.3    Fersht, A.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.