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Science 11 August 1995:
Vol. 269. no. 5225, pp. 836 - 841
DOI: 10.1126/science.7638601
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Articles

Science, Vol 269, Issue 5225, 836-841
Copyright © 1995 by American Association for the Advancement of Science

articles

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding

MK Hayer-Hartl, J Martin, and FU Hartl

Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.

The chaperonins GroEL and GroES of Escherichia coli facilitate protein folding in an adenosine triphosphate (ATP)-dependent reaction cycle. The kinetic parameters for the formation and dissociation of GroEL-GroES complexes were analyzed by surface plasmon resonance. Association of GroES and subsequent ATP hydrolysis in the interacting GroEL toroid resulted in the formation of a stable GroEL:ADP:GroES complex. The complex dissociated as a result of ATP hydrolysis in the opposite GroEL toroid, without formation of a symmetrical GroEL:(GroES)2 intermediate. Dissociation was accelerated by the addition of unfolded polypeptide. Thus, the functional chaperonin unit is an asymmetrical GroEL:GroES complex, and substrate protein plays an active role in modulating the chaperonin reaction cycle.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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The Intermediate Domain Defines Broad Nucleotide Selectivity for Protein Folding in Chlamydophila GroEL1.
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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)
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Structure of the Neisseria meningitidis Outer Membrane PilQ Secretin Complex at 12 A Resolution.
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Functional Characterization of an Archaeal GroEL/GroES Chaperonin System: SIGNIFICANCE OF SUBSTRATE ENCAPSULATION.
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Structural Plasticity and Noncovalent Substrate Binding in the GroEL Apical Domain. A STUDY USING ELECTROSPRAY IONIZATION MASS SPECTROMETRY AND FLUORESCENCE BINDING STUDIES.
A. E. Ashcroft, A. Brinker, J. E. Coyle, F. Weber, M. Kaiser, L. Moroder, M. R. Parsons, J. Jager, U. F. Hartl, M. Hayer-Hartl, et al. (2002)
J. Biol. Chem. 277, 33115-33126
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Metal ions modulate the plastic nature of Mycobacterium tuberculosis chaperonin-10.
B. Taneja and S. C. Mande (2001)
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Chaperone rings in protein folding and degradation.
A. L. Horwich, E. U. Weber-Ban, and D. Finley (1999)
PNAS 96, 11033-11040
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Disassembly of the Cytosolic Chaperonin in Mammalian Cell Extracts at Intracellular Levels of K+ and ATP.
A. Roobol, J. Grantham, H. C. Whitaker, and M. J. Carden (1999)
J. Biol. Chem. 274, 19220-19227
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Chaperone-Mediated Protein Folding.
A. L. Fink (1999)
Physiol Rev 79, 425-449
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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
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Role of the GroEL Chaperonin Intermediate Domain in Coupling ATP Hydrolysis to Polypeptide Release.
J. Martin (1998)
J. Biol. Chem. 273, 7351-7357
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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
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Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.
Y. Dubaquie, R. Looser, and S. Rospert (1997)
PNAS 94, 9011-9016
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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
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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
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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 »
Ligand-induced Conformational Changes in the Apical Domain of the Chaperonin GroEL.
D. L. Gibbons and P. M. Horowitz (1996)
J. Biol. Chem. 271, 238-243
   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
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Mechanisms and Pathways of Chaperone-mediated Protein Folding.
F.U. Hartl (1995)
Cold Spring Harb Symp Quant Biol 60, 429-434
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