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

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.