Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
摘要：
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.
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关键词：
Chloroplasts Escherichia coli Adenosine Triphosphate GroEL Protein GroES Protein Chaperonin 60 Protein Conformation Ribulose-Bisphosphate Carboxylase
DOI：
10.1038/342884a0
被引量：
年份：
1989
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