DOI: 10.1073/pnas.92.26.12021. The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.

10.1073/pnas.92.26.12021

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Chaperonins GroEL and GroES form, in the presence of ATP, two types of heterooligomers in solution: an asymmetric GroEL14GroES7 "bullet"-shaped particle and a symmetric GroEL14(GroES7)2 "football"-shaped particle. Under limiting concentrations of ATP or GroES, excess ADP, or in the presence of 5'-adenylyl imidodiphosphate, a correlation is seen between protein folding and the amount of symmetric GroEL14(GroES7)2 particles in a chaperonin solution, as detected by electron microscopy or by chemical crosslinking. Kinetic analysis suggests that protein folding is more efficient when carried out by a chaperonin solution populated with a majority of symmetric GroEL14(GroES7)2 particles than by a majority of asymmetric GroEL14GroES7 particles. The symmetric heterooligomer behaves as a highly efficient intermediate of the chaperonin protein folding cycle in vitro.

Bibliography

Azem, A., Diamant, S., Kessel, M., Weiss, C., & Goloubinoff, P. (1995). The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer. Proceedings of the National Academy of Sciences, 92(26), 12021â12025.

Authors 5

A Azem (first)
S Diamant (additional)
M Kessel (additional)
C Weiss (additional)
P Goloubinoff (additional)

References 0 Referenced 76

None

Dates

Type	When
Created	19 years, 3 months ago (May 31, 2006, 9:26 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 2:01 p.m.)
Indexed	1 week, 1 day ago (Aug. 27, 2025, 11:54 a.m.)
Issued	29 years, 8 months ago (Dec. 19, 1995)
Published	29 years, 8 months ago (Dec. 19, 1995)
Published Online	29 years, 8 months ago (Dec. 19, 1995)
Published Print	29 years, 8 months ago (Dec. 19, 1995)

Funders 0

None

BibTeX

@article{Azem_1995, title={The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.}, volume={92}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.92.26.12021}, DOI={10.1073/pnas.92.26.12021}, number={26}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Azem, A and Diamant, S and Kessel, M and Weiss, C and Goloubinoff, P}, year={1995}, month=dec, pages={12021–12025} }

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