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Science 29 July 1994:
Vol. 265. no. 5172, pp. 656 - 659
DOI: 10.1126/science.7913554
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Articles

Science, Vol 265, Issue 5172, 656-659
Copyright © 1994 by American Association for the Advancement of Science

articles

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

Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, Germany.

The particular structural arrangement of chaperonins probably contributes to their ability to assist in the folding of proteins. The interaction of the oligomeric bacterial chaperonin GroEL and its cochaperonin, GroES, in the presence of adenosine diphosphate (ADP) forms an asymmetric complex. However, in the presence of adenosine triphosphate (ATP) or its nonhydrolyzable analogs, symmetric complexes were found by electron microscopy and image analysis. The existence of symmetric chaperonin complexes is not predicted by current models of the functional cycle for GroE-mediated protein folding. Because complete folding of a nonnative substrate protein in the presence of GroEL and GroES only occurs in the presence of ATP, but not with ADP, the symmetric chaperonin complexes formed during the GroE cycle are proposed to be functionally significant.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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
   Abstract »    Full Text »    PDF »
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
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Disassembling Protein Aggregates in the Yeast Cytosol: THE COOPERATION OF HSP26 WITH SSA1 AND HSP104.
M. Haslbeck, A. Miess, T. Stromer, S. Walter, and J. Buchner (2005)
J. Biol. Chem. 280, 23861-23868
   Abstract »    Full Text »    PDF »
"Half of the Sites" Binding of D-Glyceraldehyde-3-phosphate Dehydrogenase Folding Intermediate with GroEL.
J. Li and C.-c. Wang (1999)
J. Biol. Chem. 274, 10790-10794
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »
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 »
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 »
Effects of the Inter-ring Communication in GroEL Structural and Functional Asymmetry.
O. Llorca, J. Perez-Perez, J. L. Carrascosa, A. Galan, A. Muga, and J. M. Valpuesta (1997)
J. Biol. Chem. 272, 32925-32932
   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 »
Conformational Changes at the Nucleotide Binding of GroEL Induced by Binding of Protein Substrates. LUMINESCENCE STUDIES.
J. E. Churchich (1997)
J. Biol. Chem. 272, 19645-19648
   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 »
Catalysis of protein folding by symmetric chaperone complexes.
H. Sparrer, K. Rutkat, and J. Buchner (1997)
PNAS 94, 1096-1100
   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 »
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 »
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 »
Increase of Solubility of Foreign Proteins in Escherichia coli by Coproduction of the Bacterial Thioredoxin.
T. Yasukawa, C. Kanei-Ishii, T. Maekawa, J. Fujimoto, T. Yamamoto, and S. Ishii (1995)
J. Biol. Chem. 270, 25328-25331
   Abstract »    Full Text »    PDF »
A Monomeric Variant of GroEL Binds Nucleotides but Is Inactive as a Molecular Chaperone.
Z. W. White, K. E. Fisher, and E. Eisenstein (1995)
J. Biol. Chem. 270, 20404-20409
   Abstract »    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 »
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 »
A Mutant at Position 87 of the GroEL Chaperonin Is Affected in Protein Binding and ATP Hydrolysis.
C. Weiss and P. Goloubinoff (1995)
J. Biol. Chem. 270, 13956-13960
   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 »
Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.
A Azem, M Kessel, and P Goloubinoff (1994)
Science 265, 653-656
   Abstract »    PDF »
Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding.
M. Todd, P. Viitanen, and G. Lorimer (1994)
Science 265, 659-666
   Abstract »    PDF »
Discrimination between Native and Non-native Disulfides by Protein-disulfide Isomerase.
J. Zheng and H. F. Gilbert (2001)
J. Biol. Chem. 276, 15747-15752
   Abstract »    Full Text »    PDF »


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