메뉴 건너뛰기




Volumn 293, Issue 3, 1999, Pages 667-684

A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL

Author keywords

Allostery; ATP; Chaperonins; GroEL; Transient kinetic analysis

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; NUCLEOTIDE; TRYPTOPHAN; TYROSINE;

EID: 0032714370     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3138     Document Type: Article
Times cited : (69)

References (54)
  • 5
    • 0028098798 scopus 로고
    • Direct, real-time measurement of rapid inorganic-phosphate release using a novel fluorescent probe and its application to actomyosin subfragment-1 ATPase
    • Brune M., Hunter J. L., Corrie J. E. T., Webb M. R. Direct, real-time measurement of rapid inorganic-phosphate release using a novel fluorescent probe and its application to actomyosin subfragment-1 ATPase. Biochemistry. 33:1994;8262-8271.
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, J.E.T.3    Webb, M.R.4
  • 6
    • 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
  • 7
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston S. G., Ranson N. A., Clarke A. R. The origins and consequences of asymmetry in the chaperonin reaction 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
  • 8
    • 0029823985 scopus 로고    scopus 로고
    • Release of both native and nonnative proteins from a cis-only GroEL ternary complex
    • Burston S. G., Weissman J. S., Farr G. W., Fenton W. A., Horwich A. L. Release of both native and nonnative proteins from a cis-only GroEL ternary complex. 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
  • 10
    • 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
  • 11
    • 0029864380 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and translocation
    • Clarke A. R. Molecular chaperones in protein folding and translocation. Curr. Opin. Struct. Biol. 6:1996;43-50.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 43-50
    • Clarke, A.R.1
  • 12
    • 0029664316 scopus 로고    scopus 로고
    • Towards a mechanism for GroEL.GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
    • Corrales F. J., Fersht A. R. Towards 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
  • 13
    • 0345717445 scopus 로고
    • FACSIMILE program
    • United Kingdom Atomic Energy Authority (Unclassified)
    • Curtis A. R., Sweetenham W. P. FACSIMILE program. HMSO Report AERE-R 11771. 1985;United Kingdom Atomic Energy Authority (Unclassified).
    • (1985) HMSO Report AERE-R 11771
    • Curtis, A.R.1    Sweetenham, W.P.2
  • 14
    • 0025897094 scopus 로고
    • Application of linear free energy relations to protein conformational changes: The quaternary structural changes in hemoglobin
    • Eaton W. A., Henry E. R., Hofrichter J. Application of linear free energy relations to protein conformational changes: the quaternary structural changes in hemoglobin. Proc. Natl Acad. Sci. USA. 88:1991;4472-4475.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4472-4475
    • Eaton, W.A.1    Henry, E.R.2    Hofrichter, J.3
  • 15
    • 0024554107 scopus 로고
    • The GroES and GroEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
    • Fayet O., Ziegelhoffer T., Georgopoulos C. M. The GroES and GroEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171:1989;1379-1385.
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.M.3
  • 16
    • 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
  • 17
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton W. A., Kashi 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    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 18
    • 0029731414 scopus 로고    scopus 로고
    • Intrinsic fluorescence studies of the chaperonin groEL containing single Tyr→Trp replacements reveal ligand induced conformational changes
    • Gibbons D. L., Hixson J. D., Hay N., Lund P. A., Gorovits B. M., Ybarra J., Horowitz P. M. Intrinsic fluorescence studies of the chaperonin groEL containing single Tyr→Trp replacements reveal ligand induced conformational changes. J. Biol. Chem. 271:1996;31989-31995.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31989-31995
    • Gibbons, D.L.1    Hixson, J.D.2    Hay, N.3    Lund, P.A.4    Gorovits, B.M.5    Ybarra, J.6    Horowitz, P.M.7
  • 19
    • 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
  • 20
    • 0029157195 scopus 로고
    • Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein-folding
    • Hayer-Hartl M. K., Martin J., Hartl F. U. Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein-folding. Science. 269:1995;836-841.
    • (1995) Science , vol.269 , pp. 836-841
    • Hayer-Hartl, M.K.1    Martin, J.2    Hartl, F.U.3
  • 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
  • 23
    • 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
  • 24
    • 0018791259 scopus 로고
    • Isolation and characterisation of the host protein GroE involved in bacteriophage lambda assembly
    • Hohn T., Hohn B., Engel A., Wurtz M., Smith P. R. Isolation and characterisation of the host protein GroE involved in bacteriophage lambda assembly. J. Mol. Biol. 129:1979;359-373.
    • (1979) J. Mol. Biol. , vol.129 , pp. 359-373
    • Hohn, T.1    Hohn, B.2    Engel, A.3    Wurtz, M.4    Smith, P.R.5
  • 25
    • 0027925641 scopus 로고
    • Protein folding in the cell - functions of two families of molecular chaperone, hsp60 and TF-TCP1
    • Horwich A. L., Willison K. R. Protein folding in the cell - functions of two families of molecular chaperone, hsp60 and TF-TCP1. Phil. Trans. Roy. Soc. ser. B. 339:1993;313-326.
    • (1993) Phil. Trans. Roy. Soc. Ser. B , vol.339 , pp. 313-326
    • Horwich, A.L.1    Willison, K.R.2
  • 26
    • 0030846353 scopus 로고    scopus 로고
    • Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37 °c but not 43 °c
    • Ivic A., Olden D., Wallington E. J., Lund P. A. Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37 °C but not 43 °C. Gene. 194:1997;1-8.
    • (1997) Gene , vol.194 , pp. 1-8
    • Ivic, A.1    Olden, D.2    Wallington, E.J.3    Lund, P.A.4
  • 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., Burston S. G. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle - implications for the mechanism of assisted protein folding. Biochemistry. 32:1993;2554-2563.
    • (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
    • 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
  • 29
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland D. E. Jr, Némethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry. 5:1966;365.
    • (1966) Biochemistry , vol.5 , pp. 365
    • Koshland D.E., Jr.1    Némethy, G.2    Filmer, D.3
  • 30
    • 0029875225 scopus 로고    scopus 로고
    • Nucleotide binding-promoted conformational changes release a non-native polypeptide from the Escherichia coli chaperonin GroEL
    • Lin Z. L., Eisenstein E. Nucleotide binding-promoted conformational changes release a non-native polypeptide from the Escherichia coli chaperonin GroEL. Proc. Natl Acad. Sci. USA. 93:1996;1977-1981.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1977-1981
    • Lin, Z.L.1    Eisenstein, E.2
  • 31
    • 0030766287 scopus 로고    scopus 로고
    • Protein folding - folding with a two-stroke motor
    • Lorimer G. Protein folding - folding with a two-stroke motor. Nature. 388:1997;720-723.
    • (1997) Nature , vol.388 , pp. 720-723
    • Lorimer, G.1
  • 33
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J., Wyman J., Changeux J. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:1965;88.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88
    • Monod, J.1    Wyman, J.2    Changeux, J.3
  • 34
    • 0029087065 scopus 로고
    • Chaperonins can catalyze the reversal of early aggregation steps when a protein misfolds
    • Ranson N. A., Dunster N. J., Burston S. G., Clarke A. R. Chaperonins can catalyze 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
  • 35
    • 0031557387 scopus 로고    scopus 로고
    • Binding, encapsulation and ejection: Substrate dynamics during a chaperonin-assisted folding reaction
    • Ranson N. A., Burston S. G., Clarke A. R. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction. J. Mol. Biol. 266:1997;656-664.
    • (1997) J. Mol. Biol. , vol.266 , pp. 656-664
    • Ranson, N.A.1    Burston, S.G.2    Clarke, A.R.3
  • 36
    • 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. X., 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.X.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 38
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings
    • Rye H. S., Roseman A. M., Chen S., Furtak K., Fenton W. A., Saibil H. R., Horwich A. L. GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings. Cell. 97:1999;325-338.
    • (1999) Cell , vol.97 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Chen, S.3    Furtak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 41
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • Shtilerman M., Lorimer G. H., Englander S. W. Chaperonin function: folding by forced unfolding. Science. 284:1999;822-825.
    • (1999) Science , vol.284 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 43
    • 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
  • 44
    • 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
  • 45
    • 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
  • 46
    • 0033023231 scopus 로고    scopus 로고
    • Thinking outside the box: New insights into the mechanism of GroEL-mediated protein folding
    • Wang J. D., Weissman J. S. Thinking outside the box: new insights into the mechanism of GroEL-mediated protein folding. Nature Struct. Biol. 6:1999;597-600.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 597-600
    • Wang, J.D.1    Weissman, J.S.2
  • 47
    • 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
  • 49
    • 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
  • 50
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)(7) chaperonin complex
    • Xu Z. H., Horwich A. L., Sigler P. B. The crystal structure of the asymmetric GroEL-GroES-(ADP)(7) chaperonin complex. Nature. 388:1997;741-749.
    • (1997) Nature , vol.388 , pp. 741-749
    • Xu, Z.H.1    Horwich, A.L.2    Sigler, P.B.3
  • 51
    • 0028135063 scopus 로고
    • Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala
    • Yifrach O., Horovitz A. Two lines of allosteric communication in the oligomeric chaperonin GroEL 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
  • 52
    • 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
  • 53
    • 0032546571 scopus 로고    scopus 로고
    • Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL
    • Yifrach O., Horovitz A. Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL. Biochemistry. 37:1998;7083-7088.
    • (1998) Biochemistry , vol.37 , pp. 7083-7088
    • Yifrach, O.1    Horovitz, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.