Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin

Journal of Molecular Biology

Volumn 315, Issue 1, 2002, Pages 73-85

  Yoshida, Takao ^a   Kawaguchi, Rika ^b   Taguchi, Hideki ^c   Yoshida, Masasuke ^c   Yasunaga, Takuo ^d   Wakabayashi, Takeyuki ^d   Yohda, Masafumi ^e   Maruyama, Tadashi ^a,b  

^a MARINE BIOTECHNOLOGY INSTITUTE   (Japan)

^b KITASATO UNIVERSITY   (Japan)

^c Tokyo Institute of Technology ^*  (Japan)

^d UNIVERSITY OF TOKYO   (Japan)

^e TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

Author keywords

Archaea; Central cavity; Cis folding; Group II chaperonin; Protein folding mechanism

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; CHAPERONIN; GREEN FLUORESCENT PROTEIN; OLIGOMER; RECOMBINANT PROTEIN;

ARTICLE; BACTERIAL STRAIN; BETA CHAIN; CONTROLLED STUDY; ENZYME ASSAY; GEL FILTRATION CHROMATOGRAPHY; HYDROLYSIS; INCUBATION TIME; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN FUNCTION; THERMOCOCCUS;

ARCHAEA; EUKARYOTA; HOMO; THERMOCOCCUS;

EID: 0036290267     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5220     Document Type: Article

References (48)

1. Molecular chaperones
2. Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
3. The chaperonin containing t-complex polypeptide 1 (TCP-1) multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
4. GroEL-mediated protein folding
5. Molecular chaperones in cellular protein folding
6. Structure and function in GroEL-mediated protein folding
7. Group II chaperonins: New TRiC(k)s and turns of a protein folding machine
8. Recurrent paralogy in the evolution of archaeal chaperonins
9. The crystal structure of the bacterial chaperonin GroEL at 2. 8 A
10. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
11. GroEL-GroES-mediated protein folding requires an intact central cavity
12. Thinking outside the box: New insights into the mechanism of GroEL-mediated protein folding
13. Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae
14. Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin
15. ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy
16. ATPase cycle of an archaeal chaperonin
17. ATP binding induces large conformational changes in the apical and equatorial domains of the eukaryotic chaperonin containing TCP-1 complex
18. 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin
19. Eukaryotic type II chaperonin CCT interacts with actin through specific subunits
20. The thermosome: Chaperonin with a built-in lid
21. Principles of chaperonin-assisted protein folding: Differences between in vitro and in vivo mechanisms
22. Pathway leading to correctly folded beta-tubulin
23. Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and non-native forms
24. The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro
25. Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule
26. Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability
27. Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum, Thermococcus strain KS-1
28. Corrigendum. Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum, Thermococcus strain KS-1
29. Growth requirements of hyperthermophilic sulfur-dependent heterotrophic archaea isolated from a shallow submarine geothermal system with reference to their essential amino acids
30. Natural chaperonin of the hyperthermophilic archaeum, Thermococcus strain KS-1: A hetero-oligomeric chaperonin with variable subunit composition
31. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
32. Circularly permuted variants of the green fluorescent protein
33. Chaperonin-mediated folding of green fluorescent protein
34. On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES
35. Protein folding in the central cavity of the GroEL-GroES chaperonin complex
36. Citrate synthase from the thermoplilic archaebacteria, Thermoplasma acidophilum and Sulfolobus acidcaldarius
37. Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum
38. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
39. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
40. Quasi-native chaperonin-bound intermediates in facilitated protein folding
41. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
42. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of non-native forms
43. Harmonic analysis of electron microscope images with rotational symmetry
44. Improved methods for determination of rotational symmetries in macromolecules
45. Extensible and object-oriented system Eos supplies a new environment for image analysis of electron micrographs of macromolecules
46. V-Type H + -ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon
47. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
48. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding