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Localization of prion-destabilizing mutations in the N-terminal non-prion domain of Rnq1 inSaccharomyces cerevisiae
| Content Provider | Scilit |
|---|---|
| Author | Shibata, Shoichiro Kurahashi, Hiroshi Nakamura, Yoshikazu |
| Copyright Year | 2009 |
| Description | $[PIN^{+}$] is the prion form of Rnq1 in Saccharomyces cerevisiae and is necessary for the de novo induction of a second prion, $[PSI^{+}$]. The function of Rnq1, however, is little understood. The limited availability of defective rnq1 alleles impedes the study of its structure-function relationship by genetic analysis. In this study, we isolated rnq1 mutants that are defective in the stable maintenance of the $[PIN^{+}$] prion. Since there is no rnq1 phenotype available that is applicable to a direct selection or screening for loss-of-function rnq1 mutants, we took advantage of a prion inhibitory agent, Rnq1Δ100, to develop a color-based genetic screen. Rnq1Δ100 eliminates the $[PSI^{+}$] prion in the $[PIN^{+}$] state but not in the $[pin^{-}$] state. This allows us to find $loss-of-[PIN^{+}$] rnq1 mutants as white $[PSI^{+}$] colonies. Nine rnq1 mutants with single-amino-acid substitutions were defined. These mutations impaired the stable maintenance of $[PIN^{+}$] and, as a consequence, were also partially defective in the de novo induction of $[PSI^{+}$]. Interestingly, eight of the nine alleles were mapped to the N-terminal region of Rnq1, which is known as the non-prion domain preceding the asparagine and glutamine rich prion domain of Rnq1. Notably, over-expression of these rnq1 mutant proteins restored $[PIN^{+}$] prion activity, suggesting that each of the rnq1 mutants was not completely inactive. These findings indicate that the N-terminal non-prion domain of Rnq1 harbors a potent activity to regulate the maintenance of the $[PIN^{+}$] prion. |
| Related Links | https://www.tandfonline.com/doi/pdf/10.4161/pri.3.4.10388?needAccess=true https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2807699/pdf |
| Ending Page | 258 |
| Page Count | 9 |
| Starting Page | 250 |
| ISSN | 19336896 |
| e-ISSN | 1933690X |
| DOI | 10.4161/pri.3.4.10388 |
| Journal | Prion |
| Issue Number | 4 |
| Volume Number | 3 |
| Language | English |
| Publisher | Informa UK Limited |
| Publisher Date | 2009-10-27 |
| Access Restriction | Open |
| Subject Keyword | Journal: Prion Biochemistry and Molecular Biology Mycology Rnq1 [pin+] Sup35 [psi+] Yeast Prion |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Infectious Diseases Biochemistry Cellular and Molecular Neuroscience |
