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PMID:10532860
| Citation |
Goloubinoff, P, Christeller, JT, Gatenby, AA and Lorimer, GH Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature 342:884-9 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1038/342884a0 |
| Keywords |
Adenosine Triphosphate/metabolism; Chaperonin 10/metabolism; Chaperonin 60/metabolism; Chloroplasts/enzymology; Escherichia coli; Protein Conformation; Ribulose-Bisphosphate Carboxylase/chemistry; Ribulose-Bisphosphate Carboxylase/metabolism |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
involved_in |
GO:0051085: chaperone cofactor-dependent protein refolding |
ECO:0000314: direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051085: chaperone cofactor-dependent protein refolding |
ECO:0000314: direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
Notes
See also
References
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