Nature 348, 339 - 342 (22 November 1990); doi:10.1038/348339a0

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

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

Institute of Protein Research of the Academy of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR
^*To whom correspondence should be addressed.

THE important Escherichia coli heat-shock protein GroEL of relative molecular mass 57,259 (ref. 1) is a typical molecular chaperone^2,3. It possesses ATPase activity^4,5 and interacts in ATP-driven reactions with non-folded proteins^6–8 to stimulate their correct folding and/or assembly by preventing the formation of improper protein structures or aggregates^7,9–11. As GroEL is isolated and functions as a 20–25S tetradecameric particle^5,6,12 (GroEL_p), 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 GroEL_p reassembly from its monomeric state.

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