Symmetric Complexes of GroE Chaperonins as Part of the Functional Cycle
- 29 July 1994
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 265 (5172) , 656-659
- https://doi.org/10.1126/science.7913554
Abstract
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.Keywords
This publication has 31 references indexed in Scilit:
- Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein FoldingScience, 1994
- Characterization of a Functional GroEL 14 (GroES 7 ) 2 Chaperonin Hetero-OligomerScience, 1994
- Folding Intermediate Binds to the Bottom of Bullet-shaped Holo-chaperonin and is Readily Accessible to AntibodyJournal of Molecular Biology, 1994
- The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallographyJournal of Molecular Biology, 1994
- ATP induces large quaternary rearrangements in a cage-like chaperonin structureCurrent Biology, 1993
- Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein foldingBiochemistry, 1993
- Structure of holo‐chaperonin studied with electron microscopy Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes eachFEBS Letters, 1992
- Cooperativity in ATP hydrolysis by GroEL is increased by GroESFEBS Letters, 1991
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979