Goloubinoff P, Christeller J T, Gatenby A A, Lorimer G H
Molecular Biology Division, E.I. Du Pont de Nemours & Co., Wilmington, Delaware 19880-0402, USA.
Nature. 1989;342(6252):884-9. doi: 10.1038/342884a0.
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.
来自未折叠多肽的活性核酮糖二磷酸羧化酶（Rubisco）的体外重构可由分子伴侣促进：来自大肠杆菌的伴侣蛋白60（groEL）、酵母线粒体（hsp60）或叶绿体（Rubisco亚基结合蛋白），以及来自大肠杆菌的伴侣蛋白10（groES）和Mg-ATP。由于伴侣蛋白普遍存在，因此存在一种保守的Mg-ATP依赖性机制，该机制利用伴侣蛋白促进其他一些蛋白质的折叠。
