Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
P Goloubinoff, JT Christeller, AA Gatenby, GH Lorimer - Nature, 1989 - nature.com
P Goloubinoff, JT Christeller, AA Gatenby, GH Lorimer
Nature, 1989•nature.comIn 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.
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.
Abstract
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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