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FEBS Lett. 1995 Mar 13;361(1):55-60.

In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP.

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Centre de Biochimie et Biologie Mol├ęculaire, Centre National de la Recherche Scientifique, Marseille, France.


A comparative study has investigated the in vitro dissociation and self-assembly of chaperonin 60 14-mers isolated from E. coli (GroEL), yeast mitochondria and pea chloroplasts. In all cases Mg2+ inhibits, and low temperature stimulates, the urea-induced dissociation. ATP or ADP in the presence of Mg2+ enhance the dissociation of the chaperonins. Re-assembly of the 14-mers from their monomers shows different efficiencies between the three proteins. In all cases, however, self-assembly is stimulated by Mg-adenine nucleotides. Surprisingly, effective self-assembly of GroEL is promoted by 20% glycerol in the absence of ATP. The role of Mg-adenine nucleotides in the dissociation and assembly of the chaperonins is discussed.

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