(Mg–ATP)-dependent self-assembly of molecular chaperone GroEL
- 1 November 1990
- journal article
- Published by Springer Nature in Nature
- Vol. 348 (6299) , 339-342
- https://doi.org/10.1038/348339a0
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.Keywords
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