Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded polypeptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitochondria (hsp60) 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.
Goloubinoff
P
P
Molecular Biology Division, E.I. Du Pont de Nemours & Co., Wilmington, Delaware 19880-0402, USA.
Christeller
J T
JT
Gatenby
A A
AA
Lorimer
G H
GH
D000255:Adenosine Triphosphate / Q000378:metabolism; D018835:Chaperonin 10 / Q000378:metabolism; D018834:Chaperonin 60 / Q000378:metabolism*; D002736:Chloroplasts / Q000201:enzymology; D004926:Escherichia coli; D011487:Protein Conformation; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry* / Q000378:metabolism
D018835:Chaperonin 10; D018834:Chaperonin 60; D000255:Adenosine Triphosphate; D012273:Ribulose-Bisphosphate Carboxylase