In vitro dissociation and self‐assembly of three chaperonin 60s: the role of ATP
- 7 March 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 361 (1), 55-60
- https://doi.org/10.1016/0014-5793(95)00151-x
Abstract
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.Keywords
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