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Science 29 July 1994:
Vol. 265. no. 5172, pp. 659 - 666
DOI: 10.1126/science.7913555
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Articles

Science, Vol 265, Issue 5172, 659-666
Copyright © 1994 by American Association for the Advancement of Science

articles

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

MJ Todd, PV Viitanen, and GH Lorimer

E. I. DuPont de Nemours and Company, Central Research and Development Department, Wilmington, DE 19880.

The Escherichia coli chaperonins GroEL and GroES facilitate protein folding in an adenosine triphosphate (ATP)-dependent manner. After a single cycle of ATP hydrolysis by the adenosine triphosphatase (ATPase) activity of GroEL, the bi-toroidal GroEL formed a stable asymmetric ternary complex with GroES and nucleotide (bulletlike structures). With each subsequent turnover, ATP was hydrolyzed by one ring of GroEL in a quantized manner, completely releasing the adenosine diphosphate and GroES that were tightly bound to the other ring as a result of the previous turnover. The catalytic cycle involved formation of a symmetric complex (football-like structures) as an intermediate that accumulated before the rate-determining hydrolytic step. After one to two cycles, most of the substrate protein dissociated still in a nonnative state, which is consistent with intermolecular transfer of the substrate protein between toroids of high and low affinity. A unifying model for chaperonin-facilitated protein folding based on successive rounds of binding and release, and partitioning between committed and kinetically trapped intermediates, is proposed.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.
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Triggering Protein Folding within the GroEL-GroES Complex.
D. Madan, Z. Lin, and H. S. Rye (2008)
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Setting the chaperonin timer: The effects of K+ and substrate protein on ATP hydrolysis.
J. P. Grason, J. S. Gresham, L. Widjaja, S. C. Wehri, and G. H. Lorimer (2008)
PNAS 105, 17334-17338
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Setting the chaperonin timer: A two-stroke, two-speed, protein machine.
J. P. Grason, J. S. Gresham, and G. H. Lorimer (2008)
PNAS 105, 17339-17344
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Football- and Bullet-shaped GroEL-GroES Complexes Coexist during the Reaction Cycle.
T. Sameshima, T. Ueno, R. Iizuka, N. Ishii, N. Terada, K. Okabe, and T. Funatsu (2008)
J. Biol. Chem. 283, 23765-23773
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Revisiting the GroEL-GroES Reaction Cycle via the Symmetric Intermediate Implied by Novel Aspects of the GroEL(D398A) Mutant.
A. Koike-Takeshita, M. Yoshida, and H. Taguchi (2008)
J. Biol. Chem. 283, 23774-23781
   Abstract »    Full Text »    PDF »
The ATPase Cycle of the Mitochondrial Hsp90 Analog Trap1.
A. Leskovar, H. Wegele, N. D. Werbeck, J. Buchner, and J. Reinstein (2008)
J. Biol. Chem. 283, 11677-11688
   Abstract »    Full Text »    PDF »
Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution.
R. Horst, W. A. Fenton, S. W. Englander, K. Wuthrich, and A. L. Horwich (2007)
PNAS 104, 20788-20792
   Abstract »    Full Text »    PDF »
Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.
G. W. Farr, W. A. Fenton, and A. L. Horwich (2007)
PNAS 104, 5342-5347
   Abstract »    Full Text »    PDF »
Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.
E. S. Park, W. A. Fenton, and A. L. Horwich (2007)
PNAS 104, 2145-2150
   Abstract »    Full Text »    PDF »
Elucidation of Steps in the Capture of a Protein Substrate for Efficient Encapsulation by GroE.
M. J. Cliff, C. Limpkin, A. Cameron, S. G. Burston, and A. R. Clarke (2006)
J. Biol. Chem. 281, 21266-21275
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From the Cover: Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
R. Horst, E. B. Bertelsen, J. Fiaux, G. Wider, A. L. Horwich, and K. Wuthrich (2005)
PNAS 102, 12748-12753
   Abstract »    Full Text »    PDF »
Chaperonin GroEL Meets the Substrate Protein as a "Load" of the Rings.
H. Taguchi (2005)
J. Biochem. 137, 543-549
   Abstract »    Full Text »    PDF »
BeFx Stops the Chaperonin Cycle of GroEL-GroES and Generates a Complex with Double Folding Chambers.
H. Taguchi, K. Tsukuda, F. Motojima, A. Koike-Takeshita, and M. Yoshida (2004)
J. Biol. Chem. 279, 45737-45743
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Inaugural Article: Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
F. Motojima, C. Chaudhry, W. A. Fenton, G. W. Farr, and A. L. Horwich (2004)
PNAS 101, 15005-15012
   Abstract »    Full Text »    PDF »
Identification of a Major Inter-ring Coupling Step in the GroEL Reaction Cycle.
D. Poso, A. R. Clarke, and S. G. Burston (2004)
J. Biol. Chem. 279, 38111-38117
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Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: Creation of an alternate fast folding pathway.
A. I. Jewett, A. Baumketner, and J.-E. Shea (2004)
PNAS 101, 13192-13197
   Abstract »    Full Text »    PDF »
The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104.
V. Grimminger, K. Richter, A. Imhof, J. Buchner, and S. Walter (2004)
J. Biol. Chem. 279, 7378-7383
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Dissection of the Contribution of Individual Domains to the ATPase Mechanism of Hsp90.
H. Wegele, P. Muschler, M. Bunck, J. Reinstein, and J. Buchner (2003)
J. Biol. Chem. 278, 39303-39310
   Abstract »    Full Text »    PDF »
GroEL Stability and Function: CONTRIBUTION OF THE IONIC INTERACTIONS AT THE INTER-RING CONTACT SITES.
B. Sot, S. Banuelos, J. M. Valpuesta, and A. Muga (2003)
J. Biol. Chem. 278, 32083-32090
   Abstract »    Full Text »    PDF »
Discrimination of ATP, ADP, and AMPPNP by Chaperonin GroEL: HEXOKINASE TREATMENT REVEALED THE EXCLUSIVE ROLE OF ATP.
F. Motojima and M. Yoshida (2003)
J. Biol. Chem. 278, 26648-26654
   Abstract »    Full Text »    PDF »
Salt Bridges at the Inter-ring Interface Regulate the Thermostat of GroEL.
B. Sot, A. Galan, J. M. Valpuesta, S. Bertrand, and A. Muga (2002)
J. Biol. Chem. 277, 34024-34029
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Purification and Characterization of Membrane-associated CooC Protein and Its Functional Role in the Insertion of Nickel into Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum.
W. B. Jeon, J. Cheng, and P. W. Ludden (2001)
J. Biol. Chem. 276, 38602-38609
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Human Hepatitis B Virus Polymerase Interacts with the Molecular Chaperonin Hsp60.
S. G. Park and G. Jung (2001)
J. Virol. 75, 6962-6968
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Reconstitution of Higher Plant Chloroplast Chaperonin 60 Tetradecamers Active in Protein Folding.
R. Dickson, C. Weiss, R. J. Howard, S. P. Alldrick, R. J. Ellis, G. Lorimer, A. Azem, and P. V. Viitanen (2000)
J. Biol. Chem. 275, 11829-11835
   Abstract »    Full Text »    PDF »
GroEL/GroES Promote Dissociation/Reassociation Cycles of a Heterodimeric Intermediate during alpha 2beta 2 Protein Assembly. ITERATIVE ANNEALING AT THE QUATERNARY STRUCTURE LEVEL.
R. M. Wynn, J.-L. Song, and D. T. Chuang (2000)
J. Biol. Chem. 275, 2786-2794
   Abstract »    Full Text »    PDF »
Rapid Degradation of an Abnormal Protein in Escherichia coli Proceeds through Repeated Cycles of Association with GroEL.
O. Kandror, M. Sherman, and A. Goldberg (1999)
J. Biol. Chem. 274, 37743-37749
   Abstract »    Full Text »    PDF »
A Single-Ring Mitochondrial Chaperonin (Hsp60-Hsp10) Can Substitute for GroEL-GroES In Vivo.
K. L. Nielsen, N. McLennan, M. Masters, and N. J. Cowan (1999)
J. Bacteriol. 181, 5871-5875
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On the Maximum Size of Proteins to Stay and Fold in the Cavity of GroEL underneath GroES.
C. Sakikawa, H. Taguchi, Y. Makino, and M. Yoshida (1999)
J. Biol. Chem. 274, 21251-21256
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Analysis of GroE-assisted Folding under Nonpermissive Conditions.
H. Grallert and J. Buchner (1999)
J. Biol. Chem. 274, 20171-20177
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Chaperonin Function: Folding by Forced Unfolding.
M. Shtilerman, G. H. Lorimer, and S. Walter Englander (1999)
Science 284, 822-825
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GroEL/GroES-dependent Reconstitution of alpha 2beta 2 Tetramers of Human Mitochondrial Branched Chain alpha -Ketoacid Decarboxylase. OBLIGATORY INTERACTION OF CHAPERONINS WITH AN alpha beta DIMERIC INTERMEDIATE.
J. L. Chuang, R. M. Wynn, J.-L. Song, and D. T. Chuang (1999)
J. Biol. Chem. 274, 10395-10404
   Abstract »    Full Text »    PDF »
Isolation and Characterization of a Second Subunit of Molecular Chaperonin from Pyrococcus kodakaraensis KOD1: Analysis of an ATPase-Deficient Mutant Enzyme.
M. Izumi, S. Fujiwara, M. Takagi, S. Kanaya, and T. Imanaka (1999)
Appl. Envir. Microbiol. 65, 1801-1805
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Chaperone-Mediated Protein Folding.
A. L. Fink (1999)
Physiol Rev 79, 425-449
   Abstract »    Full Text »    PDF »
GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism.
P. M. Horowitz, G. H. Lorimer, and J. Ybarra (1999)
PNAS 96, 2682-2686
   Abstract »    Full Text »    PDF »
Compensatory Changes in GroEL/Gp31 Affinity as a Mechanism for Allele-specific Genetic Interaction.
A. Richardson, S. M. van der Vies, F. Keppel, A. Taher, S. J. Landry, and C. Georgopoulos (1999)
J. Biol. Chem. 274, 52-58
   Abstract »    Full Text »    PDF »
Minimal and optimal mechanisms for GroE-mediated protein folding.
A. P. Ben-Zvi, J. Chatellier, A. R. Fersht, and P. Goloubinoff (1998)
PNAS 95, 15275-15280
   Abstract »    Full Text »    PDF »
GroEL Traps Dimeric and Monomeric Unfolding Intermediates of Citrate Synthase.
H. Grallert, K. Rutkat, and J. Buchner (1998)
J. Biol. Chem. 273, 33305-33310
   Abstract »    Full Text »    PDF »
GroEL under Heat-Shock. SWITCHING FROM A FOLDING TO A STORING FUNCTION.
O. Llorca, A. Galan, J. L. Carrascosa, A. Muga, and J. M. Valpuesta (1998)
J. Biol. Chem. 273, 32587-32594
   Abstract »    Full Text »    PDF »
GroEL-GroES-mediated protein folding requires an intact central cavity.
J. D. Wang, M. D. Michelitsch, and J. S. Weissman (1998)
PNAS 95, 12163-12168
   Abstract »    Full Text »    PDF »
Changing the Nature of the Initial Chaperonin Capture Complex Influences the Substrate Folding Efficiency.
P. A. Voziyan, B. C. Tieman, C.-M. Low, and M. T. Fisher (1998)
J. Biol. Chem. 273, 25073-25078
   Abstract »    Full Text »    PDF »
In vivo activities of GroEL minichaperones.
J. Chatellier, F. Hill, P. A. Lund, and A. R. Fersht (1998)
PNAS 95, 9861-9866
   Abstract »    Full Text »    PDF »
Type D Retrovirus Capsid Assembly and Release Are Active Events Requiring ATP.
R. A. Weldon Jr., W. B. Parker, M. Sakalian, and E. Hunter (1998)
J. Virol. 72, 3098-3106
   Abstract »    Full Text »    PDF »
Conditions for Nucleotide-dependent GroES-GroEL Interactions. GroEL14(GroES7)2 IS FAVORED BY AN ASYMMETRIC DISTRIBUTION OF NUCLEOTIDES.
B. M. Gorovits, J. Ybarra, J. W. Seale, and P. M. Horowitz (1997)
J. Biol. Chem. 272, 26999-27004
   Abstract »    Full Text »    PDF »
Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.
Y. Dubaquie, R. Looser, and S. Rospert (1997)
PNAS 94, 9011-9016
   Abstract »    Full Text »    PDF »
ATP-, K+-dependent Heptamer Exchange Reaction Produces Hybrids between GroEL and Chaperonin from Thermus thermophilus.
H. Taguchi, K. Amada, N. Murai, M. Yamakoshi, and M. Yoshida (1997)
J. Biol. Chem. 272, 18155-18160
   Abstract »    Full Text »    PDF »
How GroES Regulates Binding of Nonnative Protein to GroEL.
H. Sparrer and J. Buchner (1997)
J. Biol. Chem. 272, 14080-14086
   Abstract »    Full Text »    PDF »
Protein folding: How the mechanism of GroEL action is defined by kinetics.
C. Frieden and A. C. Clark (1997)
PNAS 94, 5535-5538
   Abstract »    Full Text »    PDF »
Mechanism of protein remodeling by ClpA chaperone.
M. Pak and S. Wickner (1997)
PNAS 94, 4901-4906
   Abstract »    Full Text »    PDF »
Chaperonin-mediated Folding of Green Fluorescent Protein.
Y. Makino, K. Amada, H. Taguchi, and M. Yoshida (1997)
J. Biol. Chem. 272, 12468-12474
   Abstract »    Full Text »    PDF »
A structural model for GroEL-polypeptide recognition.
A. M. Buckle, R. Zahn, and A. R. Fersht (1997)
PNAS 94, 3571-3575
   Abstract »    Full Text »    PDF »
Nucleotides and Two Functional States of hsp90.
W. Sullivan, B. Stensgard, G. Caucutt, B. Bartha, N. McMahon, E. S. Alnemri, G. Litwack, and D. Toft (1997)
J. Biol. Chem. 272, 8007-8012
   Abstract »    Full Text »    PDF »
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.
M. S. Goldberg, J. Zhang, S. Sondek, C. R. Matthews, R. O. Fox, and A. L. Horwich (1997)
PNAS 94, 1080-1085
   Abstract »    Full Text »    PDF »
Catalysis of protein folding by symmetric chaperone complexes.
H. Sparrer, K. Rutkat, and J. Buchner (1997)
PNAS 94, 1096-1100
   Abstract »    Full Text »    PDF »
The effect of macromolecular crowding on chaperonin-mediated protein folding.
J. Martin and F.-U. Hartl (1997)
PNAS 94, 1107-1112
   Abstract »    Full Text »    PDF »
Assisted Protein Folding.
R. W. Ruddon and E. Bedows (1997)
J. Biol. Chem. 272, 3125-3128
   Full Text »    PDF »
Dissecting intrinsic chaperonin activity.
G. M. Clore and A. M. Gronenborn (1997)
PNAS 94, 7-8
   Full Text »    PDF »
Conditions of Forming Protein Complexes with GroEL Can Influence the Mechanism of Chaperonin-assisted Refolding.
B. M. Gorovits and P. M. Horowitz (1997)
J. Biol. Chem. 272, 32-35
   Abstract »    Full Text »    PDF »
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
R. Zahn, A. M. Buckle, S. Perrett, C. M. Johnson, F. J. Corrales, R. Golbik, and A. R. Fersht (1996)
PNAS 93, 15024-15029
   Abstract »    Full Text »    PDF »
Intrinsic Fluorescence Studies of the Chaperonin GroEL Containing Single Tyr right-arrow Trp Replacements Reveal Ligand-induced Conformational Changes.
D. L. Gibbons, J. D. Hixson, N. Hay, P. Lund, B. M. Gorovits, J. Ybarra, and P. M. Horowitz (1996)
J. Biol. Chem. 271, 31989-31995
   Abstract »    Full Text »    PDF »
GroEL Locked in a Closed Conformation by an Interdomain Cross-link Can Bind ATP and Polypeptide but Cannot Process Further Reaction Steps.
N. Murai, Y. Makino, and M. Yoshida (1996)
J. Biol. Chem. 271, 28229-28234
   Abstract »    Full Text »    PDF »
Fluorescence Detection of Symmetric GroEL14(GroES7)2 Heterooligomers Involved in Protein Release during the Chaperonin Cycle.
Z. Torok, L. Vigh, and P. Goloubinoff (1996)
J. Biol. Chem. 271, 16180-16186
   Abstract »    Full Text »    PDF »
Ligand-induced Conformational Changes of GroEL Are Dependent on the Bound Substrate Polypeptide.
J. A. Mendoza and G. D. Campo (1996)
J. Biol. Chem. 271, 16344-16349
   Abstract »    Full Text »    PDF »
Autocatalytic Folding of the Folding Catalyst FKBP12.
C. Scholz, T. Zarnt, G. Kern, K. Lang, H. Burtscher, G. Fischer, and F. X. Schmid (1996)
J. Biol. Chem. 271, 12703-12707
   Abstract »    Full Text »    PDF »
GroEL Binds to and Unfolds Rhodanese Posttranslationally.
B. G. Reid and G. C. Flynn (1996)
J. Biol. Chem. 271, 7212-7217
   Abstract »    Full Text »    PDF »
Biochemical Characterization of Symmetric GroEL-GroES Complexes.
O. Llorca, J. L. Carrascosa, and J. M. Valpuesta (1996)
J. Biol. Chem. 271, 68-76
   Abstract »    Full Text »    PDF »
The Chaperonin GroEL Is Destabilized by Binding of ADP.
B. M. Gorovits and P. M. Horowitz (1995)
J. Biol. Chem. 270, 28551-28556
   Abstract »    Full Text »    PDF »
Conformational Cycle of the Archaeosome, a TCP1-like Chaperonin from Sulfolobus shibatae.
E. Quaite-Randall, J. D. Trent, R. Josephs, and A. Joachimiak (1995)
J. Biol. Chem. 270, 28818-28823
   Abstract »    Full Text »    PDF »
Prevention of in Vitro Protein Thermal Aggregation by the Sulfolobus solfataricus Chaperonin.
A. Guagliardi, L. Cerchia, and M. Rossi (1995)
J. Biol. Chem. 270, 28126-28132
   Abstract »    Full Text »    PDF »
Increased Efficiency of GroE-assisted Protein Folding by Manganese Ions.
S. Diamant, A. Azem, C. Weiss, and P. Goloubinoff (1995)
J. Biol. Chem. 270, 28387-28391
   Abstract »    Full Text »    PDF »
Quasi-native Chaperonin-bound Intermediates in Facilitated Protein Folding.
G. Tian, I. E. Vainberg, W. D. Tap, S. A. Lewis, and N. J. Cowan (1995)
J. Biol. Chem. 270, 23910-23913
   Abstract »    Full Text »    PDF »
Interactions between the GroE Chaperonins and Rhodanese.
K. E. Smith and M. T. Fisher (1995)
J. Biol. Chem. 270, 21517-21523
   Abstract »    Full Text »    PDF »
Affinity Purification, Overexpression, and Characterization of Chaperonin 10 Homologues Synthesized with and without N-terminal Acetylation.
M. T. Ryan, D. J. Naylor, N. J. Hoogenraad, and P. B. Høj (1995)
J. Biol. Chem. 270, 22037-22043
   Abstract »    Full Text »    PDF »
RNA Chaperones and the RNA Folding Problem.
D. Herschlag and D. Herschlag (1995)
J. Biol. Chem. 270, 20871-20874
   Full Text »    PDF »
Kinetic Analysis of Interactions between GroEL and Reduced alpha-Lactalbumin.
N. Murai, H. Taguchi, and M. Yoshida (1995)
J. Biol. Chem. 270, 19957-19963
   Abstract »    Full Text »    PDF »
Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.
A Engel, M. Hayer-Hartl, K. Goldie, G Pfeifer, R Hegerl, S Muller, A. da Silva, W Baumeister, and F. Hartl (1995)
Science 269, 832-836
   Abstract »    PDF »
Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.
M. Hayer-Hartl, J Martin, and F. Hartl (1995)
Science 269, 836-841
   Abstract »    PDF »
Conformational Changes Induced in the Endoplasmic Reticulum Luminal Domain of Calnexin by Mg-ATP and Ca[IMAGE].
W.-J. Ou, J. J. M. Bergeron, Y. Li, C. Y. Kang, and D. Y. Thomas (1995)
J. Biol. Chem. 270, 18051-18059
   Abstract »    Full Text »    PDF »
Functional Characterization of the Higher Plant Chloroplast Chaperonins.
P. V. Viitanen, M. Schmidt, J. Buchner, T. Suzuki, E. Vierling, R. Dickson, G. H. Lorimer, A. Gatenby, and J. Soll (1995)
J. Biol. Chem. 270, 18158-18164
   Abstract »    Full Text »    PDF »
The Molecular Chaperonin cpn60 Displays Local Flexibility That Is Reduced after Binding with an Unfolded Protein.
B. M. Gorovits and P. M. Horowitz (1995)
J. Biol. Chem. 270, 13057-13062
   Abstract »    Full Text »    PDF »
From the cradle to the grave: ring complexes in the life of a protein.
J. Weissman, P. Sigler, and A. Horwich (1995)
Science 268, 523-524
   PDF »
DsbA-mediated Disulfide Bond Formation and Catalyzed Prolyl Isomerization in Oxidative Protein Folding.
C. Frech and F. X. Schmid (1995)
J. Biol. Chem. 270, 5367-5374
   Abstract »    Full Text »    PDF »
Stability of the Asymmetric Escherichia coli Chaperonin Complex.
M. J. Todd and G. H. Lorimer (1995)
J. Biol. Chem. 270, 5388-5394
   Abstract »    Full Text »    PDF »
Mechanisms and Pathways of Chaperone-mediated Protein Folding.
F.U. Hartl (1995)
Cold Spring Harb Symp Quant Biol 60, 429-434
   Abstract »    PDF »
Kinesis of Polypeptide during GroEL-mediated Folding.
A.L. Horwich, J.S. Weissman, and W.A. Fenton (1995)
Cold Spring Harb Symp Quant Biol 60, 435-440
   Abstract »    PDF »
Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.
A Azem, M Kessel, and P Goloubinoff (1994)
Science 265, 653-656
   Abstract »    PDF »
Symmetric complexes of GroE chaperonins as part of the functional cycle.
M Schmidt, K Rutkat, R Rachel, G Pfeifer, R Jaenicke, P Viitanen, G Lorimer, and J Buchner (1994)
Science 265, 656-659
   Abstract »    PDF »
Size-dependent Disaggregation of Stable Protein Aggregates by the DnaK Chaperone Machinery.
S. Diamant, A. P. Ben-Zvi, B. Bukau, and P. Goloubinoff (2000)
J. Biol. Chem. 275, 21107-21113
   Abstract »    Full Text »    PDF »
Limits of Protein Folding Inside GroE Complexes.
H. Grallert, K. Rutkat, and J. Buchner (2000)
J. Biol. Chem. 275, 20424-20430
   Abstract »    Full Text »    PDF »
The Importance of a Mobile Loop in Regulating Chaperonin/ Co-chaperonin Interaction. HUMANS VERSUS ESCHERICHIA COLI.
A. Richardson, F. Schwager, S. J. Landry, and C. Georgopoulos (2001)
J. Biol. Chem. 276, 4981-4987
   Abstract »    Full Text »    PDF »
High Hydrostatic Pressure Can Probe the Effects of Functionally Related Ligands on the Quaternary Structures of the Chaperonins GroEL and GroES.
M. Panda, J. Ybarra, and P. M. Horowitz (2001)
J. Biol. Chem. 276, 6253-6259
   Abstract »    Full Text »    PDF »
Synchronized Domain-opening Motion of GroEL Is Essential for Communication between the Two Rings.
K. Shiseki, N. Murai, F. Motojima, T. Hisabori, M. Yoshida, and H. Taguchi (2001)
J. Biol. Chem. 276, 11335-11338
   Abstract »    Full Text »    PDF »
Chloroplasts Have a Novel Cpn10 in Addition to Cpn20 as Co-chaperonins in Arabidopsis thaliana.
Y. Koumoto, T. Shimada, M. Kondo, I. Hara-Nishimura, and M. Nishimura (2001)
J. Biol. Chem. 276, 29688-29694
   Abstract »    Full Text »    PDF »
The Disordered Mobile Loop of GroES Folds into a Defined beta -Hairpin upon Binding GroEL.
F. Shewmaker, K. Maskos, C. Simmerling, and S. J. Landry (2001)
J. Biol. Chem. 276, 31257-31264
   Abstract »    Full Text »    PDF »
Coordinated ATP Hydrolysis by the Hsp90 Dimer.
K. Richter, P. Muschler, O. Hainzl, and J. Buchner (2001)
J. Biol. Chem. 276, 33689-33696
   Abstract »    Full Text »    PDF »
Coupling between protein folding and allostery in the GroE chaperonin system.
O. Yifrach and A. Horovitz (2000)
PNAS 97, 1521-1524
   Abstract »    Full Text »    PDF »


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