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. 1990 Nov 22;348(6299):339-42.
doi: 10.1038/348339a0.

(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL

N M Lissin  1 , Venyaminov SYu, A S Girshovich
Affiliations

(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL

N M Lissin et al. Nature. .

Abstract

The important Escherichia coli heat-shock protein GroEL of relative molecular mass 57,259 is a typical molecular chaperone. It possesses ATPase activity and interacts in ATP-driven reactions with non-folded proteins to stimulate their correct folding and/or assembly by preventing the formation of improper protein structures or aggregates. As GroEL is isolated and functions as a 20-25S tetradecameric particle (GroELp), the question arises--what is the mechanism of its own assembly? Here we show the (Mg-ATP)-dependent self-stimulation ('self-chaperoning') in vitro of GroELp reassembly from its monomeric state.

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