Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes

Engel, A. and Hayer-Hartl, M. K. and Goldie, K. N. and Pfeifer, G. and Hegerl, R. and Muller, S. and da Silva, A. C. and Baumeister, W. and Hartl, F. U.. (1995) Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes. Science, Vol. 269, no. 5225. pp. 832-836.

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Official URL: http://edoc.unibas.ch/dok/A5257705

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Association for the Advancement of Science
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:22
Deposited On:22 Mar 2012 13:30

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