Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
Abstract

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.

Bibliography

Hayer-Hartl, M. K., Martin, J., & Hartl, F. U. (1995). Asymmetrical Interaction of GroEL and GroES in the ATPase Cycle of Assisted Protein Folding. Science, 269(5225), 836–841.

Authors 3
  1. Manajit K. Hayer-Hartl (first)
  2. Jörg Martin (additional)
  3. F. Ulrich Hartl (additional)
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Dates
Type When
Created 18 years, 10 months ago (Oct. 27, 2006, 2:19 p.m.)
Deposited 1 year, 7 months ago (Jan. 14, 2024, 11:53 p.m.)
Indexed 1 month, 2 weeks ago (July 11, 2025, 6:44 a.m.)
Issued 30 years ago (Aug. 11, 1995)
Published 30 years ago (Aug. 11, 1995)
Published Print 30 years ago (Aug. 11, 1995)
Funders 0

None

@article{Hayer_Hartl_1995, title={Asymmetrical Interaction of GroEL and GroES in the ATPase Cycle of Assisted Protein Folding}, volume={269}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.7638601}, DOI={10.1126/science.7638601}, number={5225}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Hayer-Hartl, Manajit K. and Martin, Jörg and Hartl, F. Ulrich}, year={1995}, month=aug, pages={836–841} }