Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.
Cell
; 100(5): 561-73, 2000 Mar 03.
Article
in En
| MEDLINE
| ID: mdl-10721993
ABSTRACT
The chaperonin GroEL binds nonnative substrate protein in the central cavity of an open ring through exposed hydrophobic residues at the inside aspect of the apical domains and then mediates productive folding upon binding ATP and the cochaperonin GroES. Whether nonnative proteins bind to more than one of the seven apical domains of a GroEL ring is unknown. We have addressed this using rings with various combinations of wild-type and binding-defective mutant apical domains, enabled by their production as single polypeptides. A wild-type extent of binary complex formation with two stringent substrate proteins, malate dehydrogenase or Rubisco, required a minimum of three consecutive binding-proficient apical domains. Rhodanese, a less-stringent substrate, required only two wild-type domains and was insensitive to their arrangement. As a physical correlate, multivalent binding of Rubisco was directly observed in an oxidative cross-linking experiment.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptides
/
Protein Binding
/
Protein Conformation
/
Ribulose-Bisphosphate Carboxylase
/
Thiosulfate Sulfurtransferase
/
Bacterial Proteins
/
Protein Folding
/
Chaperonin 60
/
Chaperonin 10
/
Malate Dehydrogenase
Limits:
Animals
Language:
En
Journal:
Cell
Year:
2000
Document type:
Article
Affiliation country: