Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

@article{Goloubinoff1989ReconstitutionOA,
  title={Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP},
  author={P. Goloubinoff and J. Christeller and A. Gatenby and G. Lorimer},
  journal={Nature},
  year={1989},
  volume={342},
  pages={884-889}
}
In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded poly-peptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitochondria (hspGO) or chloroplasts (Rubisco sub-unit-binding protein), together with chaperonin-10 from E coli(groES), and Mg-ATP. Because chaperonins are ubiquitous, a conserved Mg-ATP-dependent mechanism exists that uses the chaperonins to facilitate the folding of some other proteins. 
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