RNQ1 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

The complete DNA sequence of yeast chromosome III.
Oliver SG, van der Aart QJ, Agostoni-Carbone ML, Aigle M, Alberghina L, Alexandraki D, Antoine G, Anwar R, Ballesta JP, Benit P
Nature357(6373)38-46(1992 May)

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).
Title: [Rnq1 protein protects [PSI^(+)] prion from effect of the PNM mutation].

concluded that slow decoding of particular codons induces defects in protein homeostasis that interfere with key steps in cytokinesis and nuclear segregation
Title: Combined tRNA modification defects impair protein homeostasis and synthesis of the yeast prion protein Rnq1.

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.
Title: Cellular toxicity of yeast prion protein Rnq1 can be modulated by N-terminal wild type huntingtin.

the presence of [SWI+] can affect the interactions between Sup35 and Rnq1 during [PSI+] initiation and maturation process
Title: Investigating the interactions of yeast prions: [SWI+], [PSI+], and [PIN+].

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+].
Title: Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.