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[Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy].
N A Ryabova1, O M Selivanova1, G V Semisotnov1,2
1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.
Molekuliarnaia Biologiia
|March 8, 2018
Summary
GroEL chaperonin reassembly with GroES co-chaperonin forms one-ring heptamers initially. Later stages show one-ring and two-ring tetradecamer complexes with GroES, visualized by electron microscopy.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- GroEL chaperonin is a crucial protein folding machine.
- GroES acts as a co-chaperonin, regulating GroEL activity.
- Understanding GroEL-GroES complex formation is key to protein homeostasis.
Purpose of the Study:
- To visualize the reassembly products of GroEL chaperonin with GroES.
- To characterize the quaternary structures formed during the reaction.
- To correlate electron microscopy data with previous light scattering and electrophoresis results.
Main Methods:
- Electron microscopy was used to visualize reassembly products.
- GroEL and GroES were subjected to reassembly conditions.
- Analysis of oligomeric states and complex formation.
Main Results:
- One-ring heptameric oligomers of GroEL formed early in the reaction (~5 min).
- At later stages (~70 min), both one-ring heptamers and two-ring tetradecamers were present.
- These structures formed complexes with GroES, including asymmetrical and symmetrical forms.
Conclusions:
- The reassembly reaction proceeds through intermediate one-ring structures.
- Multiple GroEL-GroES complex stoichiometries exist at the reaction's conclusion.
- Electron microscopy provides direct visualization of these dynamic structural changes.
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