Nucleotide binding to the chaperonin GroEL: Non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1545, Issue 1-2, 2001, Pages 160-173

  Inobe, Tomonao ^a   Makio, Tadashi ^a   Takasu Ishikawa, Etsuko ^a   Terada, Tomoki P ^a   Kuwajima, Kunihiro ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Allosteric effect; Chaperonin; Cooperativity; Isothermal titration calorimetry; Nucleotide titration

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; CHAPERONIN;

ARTICLE; BINDING SITE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STRUCTURE; REACTION ANALYSIS; TITRIMETRY;

ADENINE NUCLEOTIDES; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; ALLOSTERIC REGULATION; ALLOSTERIC SITE; BINDING SITES; CALORIMETRY; FLUORESCENT DYES; GROEL PROTEIN; HYDROLYSIS; MALEIMIDES; MODELS, CHEMICAL; SPECTROMETRY, FLUORESCENCE;

EID: 0035830681     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00274-0     Document Type: Article

References (45)

1. GroEL-mediated protein folding
2. Structure and function in GroEL-mediated protein folding
3. The Hsp70 and Hsp60 chaperone machines
4. Structural aspects of GroEL function
5. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
6. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
7. Residues in chaperonin GroEL required for polypeptide binding and release
8. The hydrophobic nature of GroEL-substrate binding
9. The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state
10. Effect of GroEL on the re-folding kinetics of α-lactalbumin
11. Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL
12. Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL
13. GroEL recognises sequential and non-sequential linear structural motifs compatible with extended β-strands and α-helices
14. Cooperativity in ATP hydrolysis by GroEL is increased by GroES
15. Hydrolysis of adenosine 5′-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion
16. Chaperonin-affected refolding of α-lactalbumin: Effects of nucleotides and the co-chaperonin GroES
17. Minimal and optimal mechanisms for GroE-mediated protein folding
18. GroEL-GroES-mediated protein folding requires an intact central cavity
19. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
20. Chaperonin function: Folding by forced unfolding
21. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196Ala
22. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
23. Allosteric control by ATP of non-folded protein binding to GroEL
24. Inter-ring communication is disrupted in the GroEL mutant Arg13Gly; Ala126Val with known crystal structure
25. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
26. The origins and consequences of asymmetry in the chaperonin reaction cycle
27. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings
28. Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL
29. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL
30. Nucleotide binding-promoted conformational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL
31. Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL
32. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
33. Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for noncooperative nucleotide binding
34. In vivo analysis of integration of membrane proteins in Escherichia coli
35. GroE facilitates refolding of citrate synthase by suppressing aggregation
36. The mitochondrial protein import motor: Dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis
37. Mutation Ala2Ser destabilizes intersubunit interactions in the molecular chaperone GroEL
38. Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
39. Conformational changes at the nucleotide binding of GroEL induced by binding of protein substrates. Luminescence studies
40. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complesed with ATPγS
41. How GroES regulates binding of nonnative protein to GroEL
42. Functional communications between the apical and equatorial domains of GroEL through the intermediate domain
43. Toward a mechanism for GroEL.GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
44. ATP hydrolysis induces an intermediate conformational state in GroEL