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Related Experiment Video

Updated: Jun 15, 2025

Preparation and Cryo-FIB micromachining of Saccharomyces cerevisiae for Cryo-Electron Tomography

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Published on: November 20, 2021

Visualizing chaperonin function in situ by cryo-electron tomography.

Jonathan Wagner^1,2,3,4, Alonso I Carvajal¹, Andreas Bracher¹

¹Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.

|August 21, 2024

Summary

This summary is machine-generated.

Chaperonins like GroEL and GroES facilitate protein folding within cells. This study visualizes these complexes in situ, revealing their native cycle and how they bind and fold client proteins.

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Area of Science:

Molecular Biology
Structural Biology
Cell Biology

Background:

Chaperonins are essential molecular machines that assist protein folding.
The bacterial chaperonin GroEL, with its cofactor GroES, forms a cage-like structure for protein folding.
Previous studies relied on in vitro analyses to understand chaperonin function.

Purpose of the Study:

To determine the functional stoichiometry of GroEL, GroES, and client protein in situ.
To visualize chaperonin complexes in their natural cellular environment.
To elucidate the native reaction cycle of bacterial chaperonins.

Main Methods:

Cryo-electron tomography was used to visualize chaperonin complexes within cells.
Quantitative analysis of chaperonin complex conformations was performed.
High-resolution structures obtained in vitro were used for validation.

Main Results:

Approximately 55-70% of GroEL complexes bind GroES asymmetrically, with the remainder being symmetrical.
Substrate protein is found on the free ring of asymmetric complexes, indicating the substrate-accepting state.
Encapsulated substrate protein was observed in a folded state within GroEL-GroES chambers before release.

Conclusions:

A reaction cycle involving linked asymmetrical and symmetrical subreactions for protein folding was proposed.
The study provides direct visualization of the native conformational and functional chaperonin cycle within cells.
Findings illuminate the in vivo mechanism of ATP-dependent protein folding mediated by chaperonins.