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GroEL-mediated protein folding

W A Fenton¹, A L Horwich

¹Department of Genetics, Yale School of Medicine, New Haven, Connecticut 06510, USA.

Protein Science : a Publication of the Protein Society

|April 1, 1997

Summary

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The GroEL-GroES chaperonin system facilitates protein folding by binding nonnative polypeptides and utilizing ATP hydrolysis to drive conformational changes, ultimately releasing correctly folded proteins.

Area of Science:

Molecular Biology
Protein Folding
Chaperone Proteins

Background:

Cellular proteostasis relies on molecular chaperones to assist protein folding.
GroEL and GroES form a crucial chaperonin-cofactor system in bacteria.
Understanding the GroEL-GroES mechanism is key to comprehending protein folding pathways.

Purpose of the Study:

To elucidate the intricate architecture and reaction pathway of the GroEL-GroES chaperonin system.
To detail the mechanisms of polypeptide binding, recognition, and conformational changes induced by GroEL.
To explore the role of ATP binding and hydrolysis in driving the chaperonin-mediated folding cycle.

Main Methods:

Analysis of GroEL and GroES structure and their interaction dynamics.

Related Experiment Videos

In vitro studies investigating polypeptide binding, including hydrophobicity roles and substrate conformations.

Examination of ATP binding/hydrolysis and their influence on the chaperonin reaction cycle.

Main Results:

GroEL-GroES forms distinct cis and trans ternary complexes, with the cis complex being folding-active.
Polypeptide binding is influenced by hydrophobicity and recognized substrate conformations, including metastable intermediates.
ATP binding and hydrolysis are essential for the conformational changes driving substrate release and folding.

Conclusions:

The GroEL-GroES system employs a 'timer' mechanism, regulated by ATP, to facilitate protein folding.
Nonnative polypeptides are released during the reaction cycle, promoting proper folding.
This chaperonin system plays a vital role in maintaining cellular protein homeostasis under physiological conditions.