Nucleotide-induced transition of groel from the high-affinity to the low-affinity state for a target protein: Effects of atp and adp on the groel-affected refolding of α-lactalbumin

Journal of Molecular Biology

Volumn 312, Issue 3, 2001, Pages 555-567

  Makio, Tadashi ^a   Takasu Ishikawa, Etsuko ^a   Kuwajima, Kunihiro ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Chaperonin; Molecular chaperone; Protein folding; Stopped flow; lactalbumin

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALPHA LACTALBUMIN; CHAPERONIN; MUTANT PROTEIN; NUCLEOTIDE;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HYDROLYSIS; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN TARGETING; STEADY STATE;

EID: 0035929338     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4959     Document Type: Article

References (34)

1. Protein folding in the cell
2. Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding
3. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
4. GroEL-mediated protein folding
5. The Hsp70 and Hsp60 chaperone machines
6. + dependent
7. Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
8. Protein folding in the central cavity of the GroEL-GroES chaperonin complex
9. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
10. GroEL-GroES cycling: ATP and normative polypeptide direct alternation of folding-active rings
11. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
12. 7 chaperonin complex
13. Residues in chaperonin GroEL required for polypeptide binding and release
14. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
15. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
16. Nucleotide binding of the chaperonin GroEL: Non-co-operative binding of ATP analogs and ADP, and co-operative effect of ATP
17. Effect of GroEL on the refolding kinetics of α-lactalbumin
18. Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL
19. Toward a mechanism for GroEL·GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
20. Dynamics of the GroEL protein complex: Effects of nucleotides and folding mutants
21. Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
22. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10
23. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
24. Chaperonin-affected refolding of α-lactalbumin: Effects of nucleotides and the Co-chaperonin GroES
25. On the nature of allosteric transitions: A plausible model
26. Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for nonco-operative nucleotide binding
27. How GroES regulates binding of normative protein to GroEL
28. Coupling between protein folding and allostery in the GroE chaperonin system
29. Allosteric control by ATP of non-folded protein binding to GroEL
30. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL
31. In vivo analysis of integration of membrane proteins in Escherichia coli
32. The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state