Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene: RNQ1 - Rnq1p

Saccharomyces cerevisiae

Synonyms: Rich in asparagine and glutamine protein 1, YCL028W, YCL181, YCL28W

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Resende, C.G., Osherovich, L.Z., Meriin, A.B., Patel, B.K., Sondheimer, N., et al.

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Disease relevance of RNQ1

We screened a set of deletions of nonessential genes coding for known prions and related proteins and found that deletion of the RNQ1 gene specifically suppressed aggregation and toxicity of polyQ [1].

High impact information on RNQ1

Here, we show that the presence of prions formed by Rnq1 or Ure2 is sufficient to make cells [PIN(+)] [2].
[PSI(+)] inducibility results from gain-of-function properties of New1p and Rnq1p aggregates rather than from inactivation of the normal proteins [3].
When the prion-like region of Rnq1 was substituted for the prion domain of Sup35, the protein determinant of the prion [PSI+], the phenotypic and epigenetic behavior of [PSI+] was fully recapitulated [4].
Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1 [1].
Using a prion chimera we demonstrate that the prion-determinant domain of Rnq1 is genetically sufficient for control by Sis1 [5].

Biological context of RNQ1

In these strains a second prion gene, RNQ1, was found to be highly polymorphic, with eight different RNQ1 alleles detected in the six diploid strains studied [6].
Analysis of the naturally occurring alleles of RNQ1 and SUP35 indicated that the various polymorphisms identified were associated with DNA tandem repeats (6, 12, 33, 42 or 57 bp) within the coding sequences [6].
Unlike [PSI(+)] variants, where the strength of translation termination corresponds to the level of soluble Sup35, the phenotypes of these [PIN(+)] variants do not correspond to levels of soluble Rnq1 [7].

Associations of RNQ1 with chemical compounds

We find that the Gln/Asn-rich prion domains of two proteins, New1p and Rnq1p, can control susceptibility to [PSI(+)] induction as well as enhance aggregation of a human glutamine expansion disease protein [3].
While Rnq1p does not lose any known function upon prionization, [PIN(+)] has interesting positive phenotypes: facilitating the appearance and destabilization of other prions as well as the aggregation of polyglutamine extensions of the Huntingtin protein [8].

Other interactions of RNQ1

A specific Sis1 deletion mutant altered the physical aggregation pattern of Rnq1 without curing the prion [5].
A genetic interaction between BIK1 and SFI1 was discovered in a synthetic lethal screen using a strain deficient in the prion protein gene RNQ1 [9].

References

Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. Meriin, A.B., Zhang, X., He, X., Newnam, G.P., Chernoff, Y.O., Sherman, M.Y. J. Cell Biol. (2002)
Prions affect the appearance of other prions: the story of [PIN(+)]. Derkatch, I.L., Bradley, M.E., Hong, J.Y., Liebman, S.W. Cell (2001)
Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Osherovich, L.Z., Weissman, J.S. Cell (2001)
Rnq1: an epigenetic modifier of protein function in yeast. Sondheimer, N., Lindquist, S. Mol. Cell (2000)
The role of Sis1 in the maintenance of the [RNQ+] prion. Sondheimer, N., Lopez, N., Craig, E.A., Lindquist, S. EMBO J. (2001)
Prion protein gene polymorphisms in Saccharomyces cerevisiae. Resende, C.G., Outeiro, T.F., Sands, L., Lindquist, S., Tuite, M.F. Mol. Microbiol. (2003)
Interactions among prions and prion "strains" in yeast. Bradley, M.E., Edskes, H.K., Hong, J.Y., Wickner, R.B., Liebman, S.W. Proc. Natl. Acad. Sci. U.S.A. (2002)
"Prion-proof" for [PIN(+)]: Infection with In Vitro-made Amyloid Aggregates of Rnq1p-(132-405) Induces [PIN(+)]. Patel, B.K., Liebman, S.W. J. Mol. Biol. (2007)
Deletion of RNQ1 gene reveals novel functional relationship between divergently transcribed Bik1p/CLIP-170 and Sfi1p in spindle pole body separation. Strawn, L.A., True, H.L. Curr. Genet. (2006)