Abstract:
: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.
journal_name
Naturejournal_title
Natureauthors
Goloubinoff P,Christeller JT,Gatenby AA,Lorimer GHdoi
10.1038/342884a0keywords:
subject
Has Abstractpub_date
1989-12-21 00:00:00pages
884-9issue
6252eissn
0028-0836issn
1476-4687journal_volume
342pub_type
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