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Volumn 266, Issue 4, 1997, Pages 656-664

Binding, encapsulation and ejection: Substrate dynamics during a chaperonin-assisted folding reaction

Author keywords

Chaperonins; Malate dehydrogenase; Molecular chaperones; Protein aggregation; Protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; CHAPERONIN; MALATE DEHYDROGENASE; MITOCHONDRIAL ENZYME;

EID: 0031557387     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0815     Document Type: Article
Times cited : (81)

References (28)
  • 4
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin cycle
    • Burston S. G., Ranson N. A., Clarke A. R. The origins and consequences of asymmetry in the chaperonin cycle. J. Mol. Biol. 249:1995;138-152.
    • (1995) J. Mol. Biol. , vol.249 , pp. 138-152
    • Burston, S.G.1    Ranson, N.A.2    Clarke, A.R.3
  • 5
    • 0029823985 scopus 로고    scopus 로고
    • Native and non-native forms of a protein substrate are released from a "cis -only" form of GroEL
    • Burston S. G., Weissman J. S., Farr G. W., Fenton W. A., Horwich A. L. Native and non-native forms of a protein substrate are released from a "cis -only" form of GroEL. Nature. 383:1996;96-99.
    • (1996) Nature , vol.383 , pp. 96-99
    • Burston, S.G.1    Weissman, J.S.2    Farr, G.W.3    Fenton, W.A.4    Horwich, A.L.5
  • 6
    • 0028027055 scopus 로고
    • Location of a folding protein and shape changes in GroEL-GroES 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. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryoelectron 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
  • 7
    • 0029664316 scopus 로고    scopus 로고
    • Toward a mechanism for GroEL:GroES chaperone activity-an ATPase-gated and ATPase-pulsed folding and annealing cage
    • Corrales F. J., Fersht A. R. Toward a mechanism for GroEL:GroES chaperone activity-an ATPase-gated and ATPase-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
  • 8
    • 0026741821 scopus 로고
    • Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli. in the presence of GroEL (cpn-60) and ATP
    • Fisher M. T. Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli. in the presence of GroEL (cpn-60) and ATP. Biochemistry. 31:1992;3955-3963.
    • (1992) Biochemistry , vol.31 , pp. 3955-3963
    • Fisher, M.T.1
  • 9
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bis phosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
    • Goloubinoff P., Christeller J. T., Gatenby A. A., Lorimer G. H. Reconstitution of active dimeric ribulose bis phosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature. 342:1989;884-889.
    • (1989) Nature , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 10
    • 0027179284 scopus 로고
    • Refolding of barnase in the presence of GroEL
    • Gray T. E., Fersht A. R. Refolding of barnase in the presence of GroEL. J. Mol. Biol. 232:1993;1197-1207.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1197-1207
    • Gray, T.E.1    Fersht, A.R.2
  • 11
    • 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
  • 12
    • 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. J., Gierasch L., Deisenhoffer 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.J.3    Gierasch, L.4    Deisenhoffer, J.5
  • 13
    • 0027419011 scopus 로고
    • The 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. The binding and hydrolysis of nucleotides in the chaperonin catalytic cycle - implications for the mechanism of assisted protein folding. Biochemistry. 32:1993;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.R.6    Burston, S.G.7
  • 14
    • 0018780581 scopus 로고
    • Quaternary structure, subunit activity, and in vitro association of porcine mitochondrial malate dehydrogenase
    • Jaenicke R., Rudolph R., Heider I. Quaternary structure, subunit activity, and in vitro association of porcine mitochondrial malate dehydrogenase. Biochemistry. 18:1979;1217-1223.
    • (1979) Biochemistry , vol.18 , pp. 1217-1223
    • Jaenicke, R.1    Rudolph, R.2    Heider, I.3
  • 15
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of GroEL through a "molten globule"-like intermediate
    • Martin J., Langer T., Boteva R., Schramel A., Horwich A. L., Hartl F. U. Chaperonin-mediated protein folding at the surface of GroEL through a "molten globule"-like intermediate. Nature. 352:1991;36-42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.U.6
  • 17
    • 0026620951 scopus 로고
    • Sulphydryl modification of Escherichia coli cpn60 leads to a loss of its ability to support refolding of rhodanese but not to form a binary complex
    • Mendoza J. A., Horowitz P. M. Sulphydryl modification of Escherichia coli cpn60 leads to a loss of its ability to support refolding of rhodanese but not to form a binary complex. J. Protein Chem. 11:1992;589-594.
    • (1992) J. Protein Chem. , vol.11 , pp. 589-594
    • Mendoza, J.A.1    Horowitz, P.M.2
  • 18
    • 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., Clarke 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    Clarke, A.R.4
  • 19
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman A., Chen S., White H., Braig K., Saibil H. The chaperonin ATPase: 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.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.5
  • 20
    • 0029157314 scopus 로고
    • Interactions between the GroE chaperonins and rhodanese-multiple intermediates and release and binding
    • Smith K. E., Fisher M. T. Interactions between the GroE chaperonins and rhodanese-multiple intermediates and release and binding. J. Biol. Chem. 270:1995;21517-21523.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21517-21523
    • Smith, K.E.1    Fisher, M.T.2
  • 21
    • 0028232947 scopus 로고
    • The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding
    • Staniforth R. A., Cortès A., Burston S. G., Atkinson T., Holbrook J. J., Clarke A. R. The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding. FEBS Letters. 344:1994;129-135.
    • (1994) FEBS Letters , vol.344 , pp. 129-135
    • Staniforth, R.A.1    Cortès, A.2    Burston, S.G.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.R.6
  • 22
    • 0028855745 scopus 로고
    • Chaperonin releases the substrate protein in a form with a tendency to aggregate and ability to rebind to chaperonin
    • Taguchi H., Yoshida M. Chaperonin releases the substrate protein in a form with a tendency to aggregate and ability to rebind to chaperonin. FEBS Letters. 359:1995;195-198.
    • (1995) FEBS Letters , vol.359 , pp. 195-198
    • Taguchi, H.1    Yoshida, M.2
  • 23
    • 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
  • 24
    • 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. GroEL mediated protein folding proceeds by multiple rounds of binding and release of non-native 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
  • 26
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
    • Weissman J. S., Rye H. S., Fenton W. A., Beechem J. M., Horwich A. L. Characterization of the active intermediate of a GroEL-GroES-mediated 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    Beechem, J.M.4    Horwich, A.L.5
  • 27
    • 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
  • 28
    • 0027409438 scopus 로고
    • GroEL, GroES, and ATP dependent folding and spontaneous assembly of ornthine transcarbamylase
    • Zheng X., Rosenberg L. E., Kalousek F., Fenton W. A. GroEL, GroES, and ATP dependent folding and spontaneous assembly of ornthine transcarbamylase. J. Biol. Chem. 268:1993;7489-7493.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7489-7493
    • Zheng, X.1    Rosenberg, L.E.2    Kalousek, F.3    Fenton, W.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.