In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP.
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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Centre de Biochimie et Biologie Moléculaire, Centre National de la Recherche Scientifique, Marseille, France.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism; D003080:Cold Temperature; D004926:Escherichia coli / Q000737:chemistry; D008274:Magnesium / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D018532:Pisum sativum; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae; D014508:Urea / Q000494:pharmacology
D018834:Chaperonin 60; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D014508:Urea; D008274:Magnesium