Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

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

Nature

journal_title

Nature

authors

Goloubinoff P,Christeller JT,Gatenby AA,Lorimer GH

doi

10.1038/342884a0

keywords:

subject

Has Abstract

pub_date

1989-12-21 00:00:00

pages

884-9

issue

6252

eissn

0028-0836

issn

1476-4687

journal_volume

342

pub_type

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