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Biomolecules 2014, 4(2), 458-473;

Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition

Institute of Protein Research, Russian Academy of Sciences, Institutskaya Street 4, Pushchino 142290, Russia
Author to whom correspondence should be addressed.
Received: 10 September 2013 / Revised: 28 March 2014 / Accepted: 2 April 2014 / Published: 22 April 2014
(This article belongs to the Special Issue Protein Folding and Misfolding)
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Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself. According to the literature, GroEL reassembly is dependent on chaperonin ligands and solvent composition. Here we demonstrate dependence of GroEL reassembly efficiency on concentrations of the essential factors (Mg2+, ADP, ATP, GroES, ammonium sulfate, NaCl and glycerol). Besides, kinetics of GroEL oligomerization in various conditions was monitored by the light scattering technique and proved to be two-exponential, which suggested accumulation of a certain oligomeric intermediate. This intermediate was resolved as a heptamer by nondenaturing blue electrophoresis of GroEL monomers during their assembly in the presence of both Mg-ATP and co-chaperonin GroES. Presumably, this intermediate heptamer plays a key role in formation of the GroEL tetradecameric particle. The role of co-chaperonin GroES (Hsp10) in GroEL assembly is also discussed. View Full-Text
Keywords: oligomeric protein folding; chaperonin GroEL; denaturation; reassembly oligomeric protein folding; chaperonin GroEL; denaturation; reassembly

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Ryabova, N.; Marchenkov, V.; Kotova, N.; Semisotnov, G. Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition. Biomolecules 2014, 4, 458-473.

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