Folding of the yeast prion protein Ure2: Kinetic evidence for folding and unfolding intermediates

Journal of Molecular Biology

Volumn 315, Issue 2, 2002, Pages 213-227

  Galani, Despina ^a   Fersht, Alan R ^a   Perrett, Sarah ^a,b  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Lag phase; Off pathway; Protein folding; Protein folding pathway; Ure2p

Indexed keywords

MONOMER; PRION PROTEIN; PROTEIN URE2; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ISOMERISM; KINETICS; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0036298969     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5234     Document Type: Article

References (59)

1. Prions
2. Prions of yeast as heritable amyloidoses
3. Mad cows meet psi-chotic yeast: The expansion of the prion hypothesis
4. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast
5. [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
6. Prion domain initiation of amyloid formation in vitro from native Ure2p
7. Equilibrium folding properties of the yeast prion protein determinant Ure2
8. Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2
9. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
10. The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein
11. Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p
12. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae
13. The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p
14. The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione S-transferases
15. Stability and folding of the cell cycle regulatory protein, p13(suc1)
16. Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding
17. Movement of the position of the transition state in protein folding
18. Non-linear free energy relationships in Arc repressor unfolding imply the existence of unstable, native-like folding intermediates
19. Multiple intermediates and transition states during protein unfolding
20. Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53
21. Transient aggregates in protein folding are easily mistaken for folding intermediates
22. Transient folding intermediates characterized by protein engineering
23. The refolding of cis- and trans-peptidylprolyl isomers of barstar
24. The Greek key protein apo-pseudoazurin folds through an obligate on-pathway intermediate
25. Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
26. 1
27. A native-like intermediate on the ribonuclease A pathway. 2. Comparison of its properties to native ribonuclease
28. A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease
29. Effect of proline mutations on the stability and kinetics of folding of staphylococcal nuclease
30. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerisation of proline residues
31. Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via intermediates
32. Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra
33. Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: An amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein
34. NMR structure of the mouse prion protein domain PrP(121-321)
35. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations
36. NMR solution structure of the human prion protein
37. Variant Cretuzfeldt-Jakob disease
38. Pressure denaturation of the yeast prion protein Ure2
39. Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease
40. The energetic ups and downs of protein-folding
41. Optimization of rates of protein-folding - The nucleation-condensation mechanism and its implications
42. On-pathway versus off-pathway folding intermediates
43. Kinetic role of early intermediates in protein folding
44. A kinetically significant intermediate in the folding of barnase
45. Refolding of luciferase subunits from urea and assembly of the active heterodimer
46. Evidence for an obligatory intermediate in the folding of interleukin-1 β
47. Kinetic evidence for an obligatory intermediate in the folding of the membrane protein bacteriorhodopsin
48. Sequential domain refolding of pig muscle 3-phosphoglycerate kinase: Kinetic analysis of reactivation
49. An essential intermediate in the folding of dihydrofolate reductase
50. Self-replication and scrapie
51. Seeding "one dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
52. Nucleated conformational conversion and the replication of conformational information by a prion determinant
53. Mechansims of amyloidogenesis
54. The prion model for [URE3] of yeast: Spontaneous generation and requirements for propagation
55. The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele
56. Two prion-inducing regions of Ure2p are nonoverlapping
57. [URE3] Prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
58. Enhanced expression of the yeast Ure2 protein in Escherichia coli: The effect of synonymous codon substitutions at a selected place in the gene