The chaperonin cycle and protein folding

BioEssays

Volumn 16, Issue 4, 1994, Pages 229-231

  Lund, Peter ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CHAPERONIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEINS; PROTEIN;

ARTICLE; BIOLOGICAL MODEL; ESCHERICHIA COLI; METABOLISM; PHYSIOLOGY; PROTEIN BINDING; PROTEIN FOLDING;

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; CHAPERONINS; ESCHERICHIA COLI; GROEL PROTEIN; GROES PROTEIN; HEAT-SHOCK PROTEINS; MODELS, BIOLOGICAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEINS;

EID: 0028407344     PISSN: 02659247     EISSN: 15211878     Source Type: Journal    
DOI: 10.1002/bies.950160404     Document Type: Article

References (17)

1. The reaction cycle of GroEL and GroES in chaperonin‐assisted protein folding
2. GroE facilitates refolding of citrate synthase by suppressing aggregation
3. Principles that govern the folding of protein chains
4. Homologous plant and bacterial proteins chaperone oligomeric protein assembly
5. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends upon two chaperonin proteins and MgATP
6. Chaperonin‐mediated protein folding at the surface of GroEL through a ‘molten‐globule’ ‐like intermediate
7. Polypeptide bound to the chaperonin GroEL within a central cavity
8. Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder which accommodates the protein substrate within its central cavity
9. ATP induces large quaternary rearrangements in a cage‐like chaperonin structure
10. Purification and properties of groE, a host protein involved in bacteriophage assembly
11. The binding and hydrolysis of nucleotides in the chaperonin catalytic cycle ‐ implications for the mechanism of assisted protein folding
12. Co‐operativity in ATP hydrolysis by GroEL is increased by GroES
13. The E. coli heat‐shock proteins GroEL and GroES modulate the folding of β‐lactamase precursor
14. Binding of a chaperonin to the folding intermediates of lactate dehydrogenase
15. Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichi coli in the presence of GroEL (Chaperonin‐60) and ATP
16. Heat shock proteins and protein folding
17. + but not ATP hydrolysis