Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 11 August 1995:
Vol. 269. no. 5225, pp. 832 - 836
DOI: 10.1126/science.7638600
Prev | Table of Contents | Next

Articles

Science, Vol 269, Issue 5225, 832-836
Copyright © 1995 by American Association for the Advancement of Science

articles

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes

A Engel, MK Hayer-Hartl, KN Goldie, G Pfeifer, R Hegerl, S Muller, AC da Silva, W Baumeister, and FU Hartl

Maurice E. Muller Institute, Biozentrum, University of Basel, Switzerland.

The Escherichia coli chaperonin GroEL and its regulator GroES are thought to mediate adenosine triphosphate-dependent protein folding as an asymmetrical complex, with substrate protein bound within the GroEL cylinder. In contrast, a symmetrical complex formed between one GroEL and two GroES oligomers, with substrate protein binding to the outer surface of GroEL, was recently proposed to be the functional chaperonin unit. Electron microscopic and biochemical analyses have now shown that unphysiologically high magnesium concentrations and increased pH are required to assemble symmetrical complexes, the formation of which precludes the association of unfolded polypeptide. Thus, the functional significance of GroEL:(GroES)2 particles remains to be demonstrated.


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 »
Coexistence of Group I and Group II Chaperonins in the Archaeon Methanosarcina mazei.
D. Klunker, B. Haas, A. Hirtreiter, L. Figueiredo, D. J. Naylor, G. Pfeifer, V. Muller, U. Deppenmeier, G. Gottschalk, F. U. Hartl, et al. (2003)
J. Biol. Chem. 278, 33256-33267
   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 »
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 »
Catalysis of protein folding by symmetric chaperone complexes.
H. Sparrer, K. Rutkat, and J. Buchner (1997)
PNAS 94, 1096-1100
   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 »
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 »
Mechanisms and Pathways of Chaperone-mediated Protein Folding.
F.U. Hartl (1995)
Cold Spring Harb Symp Quant Biol 60, 429-434
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)