Structural comparison of prokaryotic and eukaryotic chaperonins

Micron

Volumn 32, Issue 1, 2001, Pages 43-50

  Carrascosa, J L ^a   Llorca, O ^a   Valpuesta, J M ^a  

^a UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

Author keywords

Atomic structure; Chaperonin; Communication mechanism; Electron microscopy; Protein folding; Structural transitions; Three dimensional reconstruction

Indexed keywords

CHAPERONIN;

ARTICLE; CHEMISTRY; COMPARATIVE STUDY; ELECTRON MICROSCOPY; EUKARYOTIC CELL; METABOLISM; METHODOLOGY; PHYSIOLOGY; PROKARYOTIC CELL; PROTEIN CONFORMATION; ULTRASTRUCTURE;

CHAPERONINS; EUKARYOTIC CELLS; MICROSCOPY, ELECTRON; PROKARYOTIC CELLS; PROTEIN CONFORMATION;

ARCHAEA; EUKARYOTA; PROKARYOTA;

EID: 0035239206     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-4328(00)00027-5     Document Type: Article

References (50)

1. The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer
2. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S
3. Chaperonins
4. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
5. A structural model for GroEL-polypeptide recognition
6. The Hsp70 and Hsp60 chaperone machines
7. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
8. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
9. Proteins as molecular chaperones
10. Residues in chaperonin GroEL required for polypeptide binding and release
11. A cytoplasmic chaperonin that catalyzes beta-actin folding
12. Two cofactors and cytoplasmic chaperonin are required for the folding of α- and β-tubulin
13. Partial occlusion of both cavities of Eukaryotic chaperonin with antibody has no effect upon the rates of β-actin and α-tubulin folding
14. Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells
15. Group II Chaperonins: New TRiC(k)s and turns of a protein folding machine
16. Molecular chaperones in cellular protein folding
17. Chaperone rings in protein folding and degradation
18. Identification of in vivo substrates of the chaperonin GroEL
19. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
20. The thermosome: Archetype of group II chaperonins
21. Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
22. Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin
23. The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
24. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
25. T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
26. The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex
27. Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes
28. Biochemical characterization of symmetric GroEL-GroES complexes Evidence for a role in protein folding
29. The formation of symmetrical GroEL-GroES complexes in the presence of ATP
30. Conformational changes in the GroEL oligomer during the functional cycle
31. Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings
32. ATP binding induces large conformational changes in the apical and equatorial domains of the eukaryotic chaperonin containing TCP-1 complex
33. 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin
34. Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
35. Reversible interaction of beta-actin along the channel of the TCP-1 cytoplasmic chaperonin
36. Group II chaperonin in an open conformation examined by electron tomography
37. The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins
38. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
39. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
40. Binding of chaperonins
41. ATP induces large quaternary rearrangements in a cage-like chaperonin structure
42. Symmetric complexes of GroE chaperonins as part of the functional cycle
43. Chaperonin function: Folding by forced unfolding
44. Structure and function in GroEL-mediated protein folding
45. The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo
46. In vivo newly translated polypeptides are sequestered in a protected folding environment
47. A yeast TCP-1-like protein is required for actin function in vivo
48. GroEL/GroES: Structure and function of a two-stroke folding machine
49. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
50. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL