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

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Abstract

THE important Escherichia coli heat-shock protein GroEL of relative molecular mass 57,259 (ref. 1) is a typical molecular chaperone2,3. It possesses ATPase activity4,5 and interacts in ATP-driven reactions with non-folded proteins6–8 to stimulate their correct folding and/or assembly by preventing the formation of improper protein structures or aggregates7,9–11. As GroEL is isolated and functions as a 20–25S tetradecameric particle5,6,12 (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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Authors and Affiliations

  1. Institute of Protein Research of the Academy of Sciences of the USSR, 142292, Pushchino, Moscow Region, USSR

    N. M. Lissin, S. Yu. Venyaminov & A. S. Girshovich

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  1. N. M. Lissin
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  2. S. Yu. Venyaminov
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  3. A. S. Girshovich
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Lissin, N., Venyaminov, S. & Girshovich, A. (Mg–ATP)-dependent self-assembly of molecular chaperone GroEL. Nature 348, 339–342 (1990). https://doi.org/10.1038/348339a0

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