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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.


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Fluorescence Detection of Symmetric GroEL14(GroES7)2 Heterooligomers Involved in Protein Release during the Chaperonin Cycle.
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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
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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
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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)
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