Recombinant Saccharomyces cerevisiae Protein URE2 (URE2)

1. DnaJB6-protected yeast cells from polyglutamine toxicity and cured yeast of both [URE3] prions and weak variants of [PSI(+)] prions but not strong [PSI(+)] prions PMID: 26702057
2. study found that, in addition to Sis1,[URE3-1] is specifically dependent upon Swa2; data suggest that prion-chaperone specificity arises from the Swa2 TPR domain and supports a model where Swa2 acts through Hsp70, most likely to provide additional access points for Hsp104 to promote prion template generation PMID: 26031938
3. Proteasomal degradation of Ure2p yields amyloidogenic N-terminal peptides and a C-terminal resistant fragment. In contrast to Sup35p, fibrillar Ure2p resists proteasomal degradation. PMID: 26115123
4. The enzymatically active microgel(URE2 protein, S cerevisiae) particles show robust material properties and their porous architecture allows diffusion in and out of reactants and products. PMID: 26030507
5. A completely disordered Ure2p prion domain implies that the amyloid formation of Ure2p, and likely other Q/N-rich yeast prion proteins, is primarily driven by inter-molecular interactions. PMID: 23077577
6. Hierarchical organization in the amyloid core of yeast prion protein Ure2. PMID: 21730048
7. Data suggest that the detailed organization of the cross-beta core of Ure2p may play an important role in the efficiency of prion propagation. PMID: 21419850
8. Ure2 enter vertebrate cells by endocytotic pathways and induce apoptosis. PMID: 20824085
9. analysis of the N-terminal domain of the prion Ure2p in isolation and in its natural context PMID: 20339590
10. The GST-encoding domain of URE2 confers arsenite resistance. PMID: 20740275
11. Results suggest that a wide variety of proteins could potentially affect [URE3] formation. PMID: 19752212
12. role of Ure2p in in vivo glutathione-mediated reactive oxygen species (ROS) scavenging was shown and that the ure2 mutation could cause significant disturbance in cellular oxidant balance and increased ROS level PMID: 19777209
13. Alignment of prion-like sequences in URE2 showed 17% similarity to human APP and 27% to human PRNP, and similar values for comparison with other mammals. PMID: 15208260
14. has glutathione peroxidase activity PMID: 15371425
15. aggregated Ure2p in [URE3] yeast cells is different from the amyloid filaments generated in vitro PMID: 15456789
16. The N-terminal prion domain of the Ure2 protein is unstructured in the soluble protein and does not have a specific interaction with the C-terminal nitrogen regulation domain. PMID: 15628874
17. Ure2 protects Saccharomyces cerevisiae from heavy metal ion and oxidative cellular damage. PMID: 15806612
18. Local area electron diffraction and X-ray diffraction from partially aligned specimens showed that the 4.7A reflection is meridional and therefore the underlying structure is cross-beta. PMID: 15866740
19. Amyloid filaments of recombinant Ure2p are nearly as infectious per mass of Ure2p as extracts of [URE3] strains. PMID: 16096644
20. prion induction by both Ure2p and Ure2-21p, one of the scrambled versions of Ure2p, is clearly dependent on the length of the inducing fragment PMID: 16123127
21. Results probe the state of Cys221 in the fibrillar form of Ure2pC221 and provide structural information on the structure of Ure2p within fibrils. PMID: 16405906
22. The relationship between structure, function and folding for the yeast prion Ure2 are discussed. PMID: 16427819
23. Ure2p is able to self-assemble into insoluble fibrils with a regularly twisted morphology. PMID: 17001037
24. no evidence was found that ageing of yeast increases the frequency of URE3 prion occurrence PMID: 17133618
25. Hsp40 (Ydj1) interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils PMID: 17324933
26. Data show that overproduction of the chaperone, Sse1p, can efficiently cure [URE3] prion propagation. PMID: 17392510
27. Results describe the conformational rearrangements that lead to the assembly of Ure2p into fibrils and the propagation of the [URE3] element in yeast. PMID: 17482207
28. cross peak intensities in 2-dimensional NMR spectra of uniformly labeled Ure2p1-89 fibrils suggests that certain portions of amino acid sequence may not participate in a rigid beta-sheet, including part of Asn-rich segment between residues 44 & 76. PMID: 17953455
29. analysis of glutathione transferase activity of the yeast prion protein Ure2 PMID: 18845158
30. J-domain point mutations that disrupt functional interactions of Ydj1p with Hsp70 abolished curing, and the J domain alone cured [URE3]. PMID: 19015537
31. the potential amyloid stretch and its preceding residue can modulate the fibril assembly of Ure2p to control the initiation of prion formation PMID: 19258323
32. Ure2 (which has no cysteine residues) also shows thiol-disulfide oxidoreductase activity similar to that of glutaredoxin enzymes. PMID: 19321443
33. These data suggest that soluble Ure2p oligomers and native-like Ure2p fibrils, but not amyloid fibrils, interact intimately with negatively charged lipid membranes, where they allow selective cation influx. PMID: 19383475
34. the spectra of full-length fibrils of Ure2p interestingly lead to highly resolved solid-state NMR spectra PMID: 19748512

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KEGG: sce:YNL229C

STRING: 4932.YNL229C