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Volumn 15, Issue 22, 1996, Pages 6111-6121

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis

Author keywords

Chaperonins; GroEL; GroES; Molecular chaperones; Protein folding

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; POLYPEPTIDE; THIOSULFATE SULFURTRANSFERASE;

EID: 0029858706     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00999.x     Document Type: Article
Times cited : (134)

References (47)
  • 1
    • 0027316898 scopus 로고
    • To fold or not to fold
    • Agard, D.A. (1993) To fold or not to fold. Science, 260, 1903-1904.
    • (1993) Science , vol.260 , pp. 1903-1904
    • Agard, D.A.1
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein using the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston, S.G., Ranson, N.A. and Clarke, A.R. (1995) The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol., 249, 138-152.
    • (1995) J. Mol. Biol. , vol.249 , pp. 138-152
    • Burston, S.G.1    Ranson, N.A.2    Clarke, A.R.3
  • 6
    • 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. and Saibil, H.R. (1994) Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron 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
  • 7
    • 0029019467 scopus 로고
    • The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding
    • Corrales, F.J. and Fersht, A.R. (1995) The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding. 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
    • 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. and Fersht, A.R. (1996) Toward a mechanism for GroEL-GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Proc. Natl Acad. Sci. USA, 93, 4509-4512.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4509-4512
    • Corrales, F.J.1    Fersht, A.R.2
  • 9
    • 0026416056 scopus 로고
    • Molecular chaperones. Unfolding protein folding
    • Creighton, T.E. (1991) Molecular chaperones. Unfolding protein folding. Nature, 352, 17-18.
    • (1991) Nature , vol.352 , pp. 17-18
    • Creighton, T.E.1
  • 10
    • 0028465426 scopus 로고
    • Molecular chaperones. Opening and closing the Anfinsen cage
    • Ellis, R.J. (1994a) Molecular chaperones. Opening and closing the Anfinsen cage. Curr. Biol., 4, 633-635.
    • (1994) Curr. Biol. , vol.4 , pp. 633-635
    • Ellis, R.J.1
  • 11
    • 0028127827 scopus 로고
    • Roles of molecular chaperones in protein folding
    • Ellis, R.J. (1994b) Roles of molecular chaperones in protein folding. Curr. Opin. Struct. Biol., 4, 117-122.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 117-122
    • Ellis, R.J.1
  • 12
    • 0030347863 scopus 로고    scopus 로고
    • Revisiting the Anfinsen cage
    • Ellis, R.J. (1996) Revisiting the Anfinsen cage. Folding & Design, 1, R9-R15.
    • (1996) Folding & Design , vol.1
    • Ellis, R.J.1
  • 13
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell: Competing models of chaperonin function
    • Ellis, R.J. and Hartl, F.U. (1996) Protein folding in the cell: competing models of chaperonin function. FASEB J., 10, 20-26.
    • (1996) FASEB J. , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.U.2
  • 15
    • 0022613101 scopus 로고
    • Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes
    • Fayet, O., Louarn, J.M. and Georgopoulos, C. (1986) Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes. Mol. Gen. Genet., 202, 435-445.
    • (1986) Mol. Gen. Genet. , vol.202 , pp. 435-445
    • Fayet, O.1    Louarn, J.M.2    Georgopoulos, C.3
  • 16
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton, W.A., Kashi, Y., Furtak, K. and 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
  • 17
    • 0025995773 scopus 로고
    • Cooperativity in ATP hydrolysis by GroEL is increased by GroES
    • Gray, T.E. and Fersht, A.R. (1991) Cooperativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Lett., 292, 254-258.
    • (1991) FEBS Lett. , vol.292 , pp. 254-258
    • Gray, T.E.1    Fersht, A.R.2
  • 18
    • 0027179284 scopus 로고
    • Refolding of barnase in the presence of GroE
    • Gray, T.E. and Fersht, A.R. (1993) Refolding of barnase in the presence of GroE. J. Mol. Biol., 232, 1197-1207.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1197-1207
    • Gray, T.E.1    Fersht, A.R.2
  • 19
    • 0027970179 scopus 로고
    • Protein folding. Secrets of a double-doughnut
    • Hartl, F.U. (1994) Protein folding. Secrets of a double-doughnut. Nature, 371, 557-559.
    • (1994) Nature , vol.371 , pp. 557-559
    • Hartl, F.U.1
  • 20
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature, 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 21
    • 0028334547 scopus 로고
    • Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin
    • Hayer-Hartl, M.K., Ewbank, J.J., Creighton, T.E. and Hartl, F.U. (1994) Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin. EMBO J., 13, 3192-3202.
    • (1994) EMBO J. , vol.13 , pp. 3192-3202
    • Hayer-Hartl, M.K.1    Ewbank, J.J.2    Creighton, T.E.3    Hartl, F.U.4
  • 22
    • 0029157195 scopus 로고
    • Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding
    • Hayer-Hartl, M.K., Martin, J. and Hartl, F.U. (1995) Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Science, 269, 836-841.
    • (1995) Science , vol.269 , pp. 836-841
    • Hayer-Hartl, M.K.1    Martin, J.2    Hartl, F.U.3
  • 23
    • 0029566336 scopus 로고
    • The role of molecular chaperones in protein folding
    • Hendrick, J. and 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.1    Hartl, F.U.2
  • 24
    • 0029127242 scopus 로고
    • Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding
    • Hlodan, R., Tempst, P. and Hartl, F.U. (1995) Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding. Nature Struct. Biol., 2, 587-595.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 587-595
    • Hlodan, R.1    Tempst, P.2    Hartl, F.U.3
  • 25
    • 0029875083 scopus 로고    scopus 로고
    • The mitochondrial protein import motor: Dissociation of mitochondrial Hsp70 from its membrane anchor requires ATP binding rather than ATP-hydrolysis
    • Horst, M., Oppliger, W., Fiefel, B., Schatz, G. and Glick, B.S. (1996) The mitochondrial protein import motor: dissociation of mitochondrial Hsp70 from its membrane anchor requires ATP binding rather than ATP-hydrolysis. Prot. Sci., 5, 759-767.
    • (1996) Prot. Sci. , vol.5 , pp. 759-767
    • Horst, M.1    Oppliger, W.2    Fiefel, B.3    Schatz, G.4    Glick, B.S.5
  • 26
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8Å resolution
    • Hunt, J.F., Weaver, A.J., Landry, S.J., Gierasch, L. and Deisenhofer, J. (1996) The crystal structure of the GroES co-chaperonin at 2.8Å resolution. Nature. 379, 37-42.
    • (1996) Nature , vol.379 , pp. 37-42
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.J.3    Gierasch, L.4    Deisenhofer, J.5
  • 27
    • 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. and 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.R.6    Burston, S.G.7
  • 28
    • 0027092285 scopus 로고
    • Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
    • Langer, T., Pfeifer, G., Martin, J., Baumeister, W. and Hartl, F.U. (1992) Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J., 11, 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
  • 29
    • 0028340341 scopus 로고
    • The formation of symmetrical GroEL-GroES complexes in the presence of ATP
    • Llorca, O., Marco, S., Carrascosa, J.L. and Valpuesta, J.M. (1994) The formation of symmetrical GroEL-GroES complexes in the presence of ATP. FEBS Lett., 345, 181-186.
    • (1994) FEBS Lett. , vol.345 , pp. 181-186
    • Llorca, O.1    Marco, S.2    Carrascosa, J.L.3    Valpuesta, J.M.4
  • 30
    • 0030031059 scopus 로고    scopus 로고
    • The structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
    • Mande, S.C., Mehra, V., Bloom, B. and Hol, W.G.J. (1996) The structure of the heat shock protein chaperonin-10 of Mycobacterium leprae. Science, 271, 203-207.
    • (1996) Science , vol.271 , pp. 203-207
    • Mande, S.C.1    Mehra, V.2    Bloom, B.3    Hol, W.G.J.4
  • 31
    • 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. and Hartl, F.U. (1991) Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature, 352, 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
  • 32
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
    • Martin, J., Mayhew, M., Langer, T. and Hartl, F.U. (1993) 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
  • 34
    • 0025820393 scopus 로고
    • Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese
    • Mendoza, J.A., Rogers, E., Lorimer, G.H. and Horowitz, P.M. (1991) Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. 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
  • 35
    • 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. and Clarke, A.R. (1995) Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds. J. Mol. Biol., 250, 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
  • 36
    • 13244295644 scopus 로고
    • ATP induces large quaternary rearrangements in a cage-like chaperonin structure
    • Saibil, H.R. et al. (1993) ATP induces large quaternary rearrangements in a cage-like chaperonin structure. Curr. Biol., 3, 265-273.
    • (1993) Curr. Biol. , vol.3 , pp. 265-273
    • Saibil, H.R.1
  • 37
    • 0028290816 scopus 로고
    • On the role of groES in the chaperonin-assisted folding reaction. Three case studies
    • Schmidt, M., Buchner, J., Todd, M.J., Lorimer, G.H. and Viitanen, P.V. (1994a) On the role of groES in the chaperonin-assisted folding reaction. Three case studies. J. Biol. Chem., 269, 10304-10311.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10304-10311
    • Schmidt, M.1    Buchner, J.2    Todd, M.J.3    Lorimer, G.H.4    Viitanen, P.V.5
  • 39
    • 0023030976 scopus 로고
    • Detergent-assisted refolding of guanidinium chloride-denatured rhodanese
    • Tandon, S. and Horowitz, P.M. (1986) Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. J. Biol. Chem., 261, 15615-15681.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15615-15681
    • Tandon, S.1    Horowitz, P.M.2
  • 40
    • 0027250447 scopus 로고
    • Hydrolysis of adenosine 5′-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion
    • Todd, M.J., Viitanen, P.V. and Lorimer, G.H. (1993) Hydrolysis of adenosine 5′-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. Biochemistry, 32, 8560-8567.
    • (1993) Biochemistry , vol.32 , pp. 8560-8567
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 41
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd, M.J., Viitanen, P.V. and 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, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 42
    • 0030006212 scopus 로고    scopus 로고
    • Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
    • Todd, M.J., Lorimer, G.H. and Thirumalai, D. (1996) Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc. Natl Acad. Sci. USA, 93, 4030-4035.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4030-4035
    • Todd, M.J.1    Lorimer, G.H.2    Thirumalai, D.3
  • 43
    • 0000366607 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA. 79, 267-271.
    • (1979) Proc. Natl Acad. Sci. USA , vol.79 , pp. 267-271
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 44
    • 0024334643 scopus 로고
    • Luminiscent immunodetection of western-blotted proteins from Coomassie-stained polyacrylamide gel
    • Vachereau, A. (1989) Luminiscent immunodetection of western-blotted proteins from Coomassie-stained polyacrylamide gel. Anal. Biochem., 179, 206-208.
    • (1989) Anal. Biochem. , vol.179 , pp. 206-208
    • Vachereau, A.1
  • 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. and 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
  • 47
    • 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. and Horwich, A.L. (1996) Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell, 84, 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


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