Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1989-12

AUTHORS

Pierre Goloubinoff, John T. Christeller, Anthony A. Gatenby, George H. Lorimer

ABSTRACT

In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded poly-peptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitochondria (hspGO) 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. More... »

PAGES

884-889

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/342884a0

DOI

http://dx.doi.org/10.1038/342884a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034565462

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10532860


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