GroEL/GroES-mediated folding of a protein too large to be encapsulated

Cell

Volumn 107, Issue 2, 2001, Pages 235-246

  Chaudhuri, Tapan K ^a,b   Farr, George W ^a,b   Fenton, Wayne A ^b   Rospert, Sabine ^c   Horwich, Arthur L ^a,b  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; HOLOENZYME; MONOMER;

ARTICLE; CONTROLLED STUDY; ENCAPSULATION; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; SOLUTION AND SOLUBILITY; YEAST;

EID: 0035913910     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(01)00523-2     Document Type: Article

References (38)

1. A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar
2. Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro
3. Release of both native and non-native proteins from a cis-only GroEL ternary complex
4. 2 tetramers of human mitochondrial branched chain α-ketoacid decarboxylase
5. The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases
6. GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism
7. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10
8. In vivo observation of polypeptide flux through the bacterial chaperonin system
9. Multivalent binding of nonnative substrate protein by the chaperonin GroEL
10. GroEL-substrate interactions: Molding the fold, or folding the mold
11. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP
12. Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural protein
13. Structural aspects of GroEL function
14. Identification of in vivo substrates of the chaperonin GroEL
15. Mechanisms for GroEL/GroES-mediated folding of a large 86-kDa fusion polypeptide in vitro
16. GroEL-assisted refolding of adrenodoxin during chemical cluster insertion
17. 2- of aconitase during cluster interconversions and removal
18. Mössbauer studies of aconitase: Substrate and inhibitor binding, reaction intermediates, and hyperfine interactions of reduced 3Fe and 4Fe clusters
19. Crystal structures of aconitase with isocitrate and nitroisocitrate bound
20. Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate
21. The activation of aconitase by ferrous ions and reducing agents
22. Chaperonins can catalyze the reversal of early aggregation steps when a protein misfolds
23. Binding, encapsulation, and ejection: Substrate dynamics during a chaperonin-assisted folding reaction
24. The chaperone GroEL is required for the final assembly of the molybdenum-iron protein of nitrogenase
25. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
26. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
27. GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings
28. Structure and function in GroEL-mediated protein folding
29. 2 assembly of mitochondrial branched-chain α-ketoacid dehydrogenase
30. Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
31. A thermodynamic coupling mechanism for GroEL-mediated unfolding
32. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
33. Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
34. 7 complex
35. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
36. Allosteric control by ATP of non-folded protein binding to GroEL
37. Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL II. GroEL recognizes thermally unfolded mature beta-lactamase
38. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB