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Volumn 1599, Issue 1-2, 2002, Pages 45-55

Nested MWC model describes hydrolysis of GroEL without assuming negative cooperativity in binding

Author keywords

ATP hydrolysis; Conformation; Cooperativity; Folding; GroEL; Nucleotide binding

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; ADENOSINE 5' O (3 THIOTRIPHOSPHATE); ADENOSINE 5'-O-(3-THIOTRIPHOSPHATE); DRUG DERIVATIVE;

EID: 0037163402     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(02)00399-0     Document Type: Article
Times cited : (7)

References (43)
  • 1
    • 0029566336 scopus 로고
    • The role of molecular chaperones in protein folding
    • Hendrick J.P., Hartl F.U. The role of molecular chaperones in protein folding. FASEB J. 9:1995;1559-1569.
    • (1995) FASEB J. , vol.9 , pp. 1559-1569
    • Hendrick, J.P.1    Hartl, F.U.2
  • 2
    • 0030050614 scopus 로고    scopus 로고
    • A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo
    • Lorimer G. A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo. FASEB J. 10:1996;1-5.
    • (1996) FASEB J. , vol.10 , pp. 1-5
    • Lorimer, G.1
  • 3
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: Functional principles of molecular chaperones
    • Buchner J. Supervising the fold: functional principles of molecular chaperones. FASEB J. 10:1996;10-19.
    • (1996) FASEB J. , vol.10 , pp. 10-19
    • Buchner, J.1
  • 5
    • 0033602228 scopus 로고    scopus 로고
    • Molecular chaperones: Pathways and networks
    • Ellis R.J. Molecular chaperones: pathways and networks. Curr. Biol. 9:1999;R137-R139.
    • (1999) Curr. Biol. , vol.9 , pp. 137-R139
    • Ellis, R.J.1
  • 7
    • 0035800783 scopus 로고    scopus 로고
    • The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivation
    • Bhattacharyya A.M., Horovitz P.M. The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivation. J. Biol. Chem. 276:2001;28739-28743.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28739-28743
    • Bhattacharyya, A.M.1    Horovitz, P.M.2
  • 9
    • 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
  • 10
    • 0035783391 scopus 로고    scopus 로고
    • Review: A structural view of the GroE chaperone cycle
    • Grallert H., Buchner J. Review: a structural view of the GroE chaperone cycle. J. Struct. Biol. 135:2001;95-103.
    • (2001) J. Struct. Biol. , vol.135 , pp. 95-103
    • Grallert, H.1    Buchner, J.2
  • 11
    • 0027250447 scopus 로고
    • Hydrolysis of ATP by E. coli GroEL: Effects of GroES and potassium
    • Todd M.J., Viitanen P.V., Lorimer G.H. Hydrolysis of ATP by E. coli GroEL: effects of GroES and potassium. Biochemistry. 32:1993;8560-8567.
    • (1993) Biochemistry , vol.32 , pp. 8560-8567
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 12
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity of the oligomeric chaperonine GroEL
    • Yifrach O., Horowitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonine GroEL. Biochemistry. 34:1995;5303-5308.
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horowitz, A.2
  • 13
    • 0028609655 scopus 로고
    • Residue Lys-34 on GroES modulates allosteric transitions in GroEL
    • Kovalenko O., Yifrach O., Horowitz A. Residue Lys-34 on GroES modulates allosteric transitions in GroEL. Biochemistry. 33:1994;14974-14978.
    • (1994) Biochemistry , vol.33 , pp. 14974-14978
    • Kovalenko, O.1    Yifrach, O.2    Horowitz, A.3
  • 14
    • 0029877893 scopus 로고    scopus 로고
    • Inter-ring communication is disrupted in the GroEL mutant Arg13→Gly, Ala126→Val with known crystal structure
    • Aharoni A., Horowitz A. Inter-ring communication is disrupted in the GroEL mutant Arg13→Gly, Ala126→Val with known crystal structure. J. Mol. Biol. 258:1996;732-735.
    • (1996) J. Mol. Biol. , vol.258 , pp. 732-735
    • Aharoni, A.1    Horowitz, A.2
  • 15
    • 0030827121 scopus 로고    scopus 로고
    • GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroES-GroEL complex
    • Inbar E., Horowitz A. GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroES-GroEL complex. Biochemistry. 36:1997;12276-12281.
    • (1997) Biochemistry , vol.36 , pp. 12276-12281
    • Inbar, E.1    Horowitz, A.2
  • 16
    • 0035929338 scopus 로고    scopus 로고
    • Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: Effects of ATP and ADP on the GroEL-affected refolding of alpha-lactalbumin
    • Makio T., Takasu-Ishikawa E., Kuwajima K. Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: effects of ATP and ADP on the GroEL-affected refolding of alpha-lactalbumin. J. Mol. Biol. 312:2001;555-567.
    • (2001) J. Mol. Biol. , vol.312 , pp. 555-567
    • Makio, T.1    Takasu-Ishikawa, E.2    Kuwajima, K.3
  • 17
    • 0035815699 scopus 로고    scopus 로고
    • Synchronized domain-opening motion of GroEL is essential for communication between the two rings
    • Shiseki K., Murai N., Motohia F., Hisabori T., Yoshida M., Taguchi H. Synchronized domain-opening motion of GroEL is essential for communication between the two rings. J. Biol. Chem. 276:2001;11335-11338.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11335-11338
    • Shiseki, K.1    Murai, N.2    Motohia, F.3    Hisabori, T.4    Yoshida, M.5    Taguchi, H.6
  • 18
    • 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. Nat. Struct. Biol. 2:1995;1-4.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1-4
    • Braig, K.1    Adams, P.D.2    Brünger, A.T.3
  • 19
  • 21
    • 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., 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.J.3    Gierasch, L.4    Deisenhofer, J.5
  • 22
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonine 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 chaperonine 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
  • 23
    • 0035783162 scopus 로고    scopus 로고
    • Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy
    • Roseman A.M., Ranson N.A., Gowen B., Fuller S.D., Saibil H.R. Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy. J. Struct. Biol. 135:2001;115-125.
    • (2001) J. Struct. Biol. , vol.135 , pp. 115-125
    • Roseman, A.M.1    Ranson, N.A.2    Gowen, B.3    Fuller, S.D.4    Saibil, H.R.5
  • 24
    • 0034665864 scopus 로고    scopus 로고
    • A dynamic model for the allosteric mechanism of GroEL
    • Ma J., Sigler P.B., Karplus M. A dynamic model for the allosteric mechanism of GroEL. J. Mol. Biol. 302:2000;303-313.
    • (2000) J. Mol. Biol. , vol.302 , pp. 303-313
    • Ma, J.1    Sigler, P.B.2    Karplus, M.3
  • 25
    • 0028135063 scopus 로고
    • Two lines of allosteric communications in the oligomeric chaperonine GroEL are revealed by the single mutation Arg196→Ala
    • Yifrach O., Horowitz A. Two lines of allosteric communications in the oligomeric chaperonine 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    Horowitz, A.2
  • 26
    • 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
  • 27
    • 0028908139 scopus 로고
    • Cooperativity in enzyme function: Equilibrium and kinetic aspects
    • Neet K.E. Cooperativity in enzyme function: equilibrium and kinetic aspects. Methods Enzymol. 249:1995;519-567.
    • (1995) Methods Enzymol. , vol.249 , pp. 519-567
    • Neet, K.E.1
  • 28
    • 0030018794 scopus 로고    scopus 로고
    • 2 heterooligomers involved in protein release during the chaperonin cycle
    • 2 heterooligomers involved in protein release during the chaperonin cycle. J. Biol. Chem. 271:1996;16180- 16186.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16180-16186
    • Török, Z.1    Vigh, L.2    Goloubinoff, P.3
  • 29
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston G., Ranson N.A., Clark 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, G.1    Ranson, N.A.2    Clark, A.R.3
  • 30
    • 0027419011 scopus 로고
    • Binding and hydrolysis of nucleotides in the chaperonine 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 chaperonine 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
  • 31
    • 0032932922 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for non-cooperative nucleotide binding
    • Terada T.P., Kuwajima K. Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: evidence for non-cooperative nucleotide binding. Biochim. Biophys. Acta. 1431:1999;269-281.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 269-281
    • Terada, T.P.1    Kuwajima, K.2
  • 32
    • 0035830681 scopus 로고    scopus 로고
    • Nucleotide binding to the chaperonin GroEL: Non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP
    • Inobe T., Makio T., Takasu-Ishikawa E., Terada T.P., Kuwajima K. Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP. Biochim. Biophys. Acta. 1545:2001;160-173.
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 160-173
    • Inobe, T.1    Makio, T.2    Takasu-Ishikawa, E.3    Terada, T.P.4    Kuwajima, K.5
  • 34
    • 0242478477 scopus 로고
    • Nesting - An extension of the allosteric model and its application to tarantula hemocyanin
    • B. Linzen. Heidelberg: Springer Verlag
    • Decker H., Robert C.H., Gill S.J. Nesting - an extension of the allosteric model and its application to tarantula hemocyanin. Linzen B. Invertebrate Oxygen Carrier. 1986;383-388 Springer Verlag, Heidelberg.
    • (1986) Invertebrate Oxygen Carrier , pp. 383-388
    • Decker, H.1    Robert, C.H.2    Gill, S.J.3
  • 35
    • 0024280217 scopus 로고
    • Nested allosteric interaction in tarantula hemocyanin revealed through the binding of oxygen and carbon monoxide
    • Decker H., Connelly P., Robert C.H., Gill S.J. Nested allosteric interaction in tarantula hemocyanin revealed through the binding of oxygen and carbon monoxide. Biochemistry. 27:1988;6901-6908.
    • (1988) Biochemistry , vol.27 , pp. 6901-6908
    • Decker, H.1    Connelly, P.2    Robert, C.H.3    Gill, S.J.4
  • 36
    • 0025070320 scopus 로고
    • Nested allostery of arthropodan hemocyanin (Eurypelma californicum and Homarus americanus): The role of the protons
    • Decker H., Sterner R. Nested allostery of arthropodan hemocyanin (Eurypelma californicum and Homarus americanus): the role of the protons. J. Mol. Biol. 211:1990;281-293.
    • (1990) J. Mol. Biol. , vol.211 , pp. 281-293
    • Decker, H.1    Sterner, R.2
  • 37
    • 0030050922 scopus 로고    scopus 로고
    • Theory of allosteric effects in serine proteases
    • Di Cera E., Hopfner K.P., Dang Q.D. Theory of allosteric effects in serine proteases. Biophys. J. 70:1996;174-181.
    • (1996) Biophys. J. , vol.70 , pp. 174-181
    • Di Cera, E.1    Hopfner, K.P.2    Dang, Q.D.3
  • 38
    • 78651189765 scopus 로고
    • On the nature of allosteric transition: A plausible model
    • Monod J., Wyman J., Changeux J.-P. On the nature of allosteric transition: a plausible model. J. Mol. Biol. 12:1965;88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 40
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland D.E., Nemethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry. 5:1966;365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Nemethy, G.2    Filmer, D.3
  • 41
    • 0018792472 scopus 로고
    • Allosteric properties and the association equilibria of hemocyanin from Callianassa californiensis
    • Arisaka F., van Holde K.E. Allosteric properties and the association equilibria of hemocyanin from Callianassa californiensis. J. Mol. Biol. 134:1979;41-73.
    • (1979) J. Mol. Biol. , vol.134 , pp. 41-73
    • Arisaka, F.1    Van Holde, K.E.2
  • 42
    • 0035907116 scopus 로고    scopus 로고
    • Two types of urate binding sites on hemocyanin from the crayfish Astacus leptodactylus: An ITC study
    • Hellmann N., Jaenicke E., Decker H. Two types of urate binding sites on hemocyanin from the crayfish Astacus leptodactylus: an ITC study. Biophys. Chem. 90:2001;279-299.
    • (2001) Biophys. Chem. , vol.90 , pp. 279-299
    • Hellmann, N.1    Jaenicke, E.2    Decker, H.3
  • 43
    • 0000166289 scopus 로고
    • Treatment of enzyme kinetic data
    • Frieden C. Treatment of enzyme kinetic data. J. Biol. Chem. 239:1964;3522-3531.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3522-3531
    • Frieden, C.1


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