Recombinant Saccharomyces cerevisiae [PIN+] prion protein RNQ1 (RNQ1)

1. concluded that slow decoding of particular codons induces defects in protein homeostasis that interfere with key steps in cytokinesis and nuclear segregation PMID: 28281930
2. results show that the presence of Rnq1p in the cell significantly decreases the loss of [PSI;(+)] prion, which is caused by a double mutation in SUP35 (Q61K, Q62K substitutions in the Sup35 protein). PMID: 28537243
3. Taking into account the earlier reports of the beneficial effect of expression of N-wt-Htt on the aggregation of mutant huntingtin, the function of wild-type huntingtin as an inhibitor of protein aggregation in the cell needs to be explored. PMID: 26628321
4. the presence of [SWI+] can affect the interactions between Sup35 and Rnq1 during [PSI+] initiation and maturation process PMID: 24727082
5. Study describes a spectrum of prion variants occurring naturally in wild yeast. all of the [RNQ+] variants characterized were efficient inducers of [PSI+], but differed in the subset of [PSI+] variants that formed and [RNQ+] structures can be modified after inducing, or interacting with, [PSI+] and in some cases, this interaction resulted in the loss of [RNQ+]. PMID: 24673812
6. Polymorphism of RNQ1 was selected to protect cells from detrimental effects of the [PIN+] prion. PMID: 22949655
7. Data indicate that the majority of mutated residues are mapped to the surface, and on one side, of contiguous alpha-helices of the nonprion domain of Rnq1, suggesting its involvement in interactions with a prion or a factor necessary for prion developmentt PMID: 21453425
8. Data suggest that transient Hsp104 overproduction enhances prion generation through persistent effects on Rnq1 amyloid, as well as by disassembly of amorphous Ure2 aggregates, driving the aggregation toward the amyloid pathway. PMID: 21467567
9. polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis PMID: 20224794
10. Differences exist in the ability of the [RNQ(+)] prion variants to faithfully propagate themselves and to template the aggregation of other proteins. PMID: 20442412
11. These findings indicate that the N-terminal non-prion domain of Rnq1 harbors a potent activity to regulate the maintenance of the [PIN(+)] prion. PMID: 20009538
12. The [RNQ1Delta100(+)] prion demonstrates selfish activity to eliminate a heterologous prion in S. cerevisiae, showing the first instance of a selfish prion variant in living organisms. PMID: 19371377
13. Rnq1 encompasses multiple prion determinants that can independently drive amyloid formation in vitro. PMID: 20107602
14. Data show that increasing heat-shock protein 40 chaperone Sis1 activity before Rnq1-GFP expression, shifted Rnq1-GFP aggregation from the cytosol to the nucleus. PMID: 19656852
15. We report that a null rnq1 mutation in the yeast RNQ1 (YCL028w) prion-like gene of so far unknown function produces the doubling of spores in the asci. PMID: 16356475
16. RNQ1 deletion reduced expression from the divergently transcribed BIK1, allowing the identification of genetic interactors with bik1. PMID: 16972090
17. analysis of the Rnq1 prion domain cross-seeding interactions with Sup35NM PMID: 17121829
18. Data report that, upon depletion of Sis1, as well as upon inactivation of Hsp104, Rnq1 aggregates increased in size. PMID: 17673909
19. use of NMR methods to examine amyloid formed in vitro from recombinant Rnq1 prion domain (residues 153-405) labeled with Tyr-1-(13)C (14 residues), Leu-1-(13)C (7 residues), or Ala-3-(13)C (13 residues) PMID: 18268327
20. the nonprion domain of Rnq1 plays a crucial role in self-regulation of the highly reactive QN-rich prion domain of Rnq1 PMID: 18332119
21. the J-protein Sis1, the Hsp70 Ssa, and the AAA+ ATPase Hsp104, act sequentially in the fragmentation of yeast prions [PSI(+)], [RNQ(+)], and [URE3], but the threshold of Sis1 activity required for each prion varies PMID: 18955697
22. These data are consistent with a model of [PSI+] induction caused by physical interactions between Rnq1p and Sup35p. PMID: 19324054
23. This study supports the occurrence of in vivo cross-seeding between Sup35 and Rnq1 and provides a new tool that can be used to dissect the mechanism of the de novo appearance of prions. PMID: 19411620
24. Results for fibrils formed by the prion protein Rnq1 support an in-register parallel beta-sheet structure, with one Rnq1 molecule per 0.47-nm beta-sheet repeat spacing. PMID: 19706519

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KEGG: sce:YCL028W

STRING: 4932.YCL028W