| Standard Name | RNQ1 1 |
|---|---|
| Systematic Name | YCL028W |
| Feature Type | ORF, Verified |
| Description | [PIN(+)] prion, an infectious protein conformation that is generally an ordered protein aggregate (1, 2 and see Summary Paragraph) Also known as: [PIN(+)] |
| Name Description | Rich in asparagine (N) and glutamine (Q) 1 |
| Chromosomal Location | |
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| View Computational GO annotations for RNQ1 | |
| Molecular Function | |
| Manually curated |
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| Biological Process | |
| Manually curated |
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| Cellular Component | |
| Manually curated |
| Classical genetics | |
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| null |
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| overexpression | |
| Large-scale survey | |
| null |
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| overexpression | |
| Resources |
| 107 total interaction(s) for 83 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| This feature contains embedded feature(s): YCLX06C | |||||||||||||
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| Last Update | Coordinates: 2000-09-13 | Sequence: 2000-09-13 | ||||||||||||
| Subfeature details |
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| S288C only | |
|---|---|
| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000000533 |
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The [PSI+] prion determinant causes nonsense suppressor phenotype due to a reduced function of the translation termination factor Sup35p (eRF3) polymerized into amyloid fibrils. Prion state of the Rnq1 protein, [PIN+], is required for the [PSI+] de novo generation, but not propagation. Yeast [psi-] [PIN+] cells overproducing Sup35p can exhibit nonsense suppression without generation of a stable [PSI+]. In such cells most of Sup35p is present in amyloid polymers, though remaining Sup35p monomer is sufficient for normal translation termination. Presence of these polymers strictly depends on [PIN+], suggesting that their maintenance relies on efficient generation de novo, rather than inheritance. Sup35p polymers contain Rnq1p, confirming that Rnq1p polymers seed Sup35p polymerization (3).
| 1) | Sondheimer N and Lindquist S (2000) Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 5(1):163-72 |
| 2) | Derkatch IL, et al. (2004) Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci U S A 101(35):12934-9 |
| 3) | Salnikova AB, et al. (2005) Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 280(10):8808-12 |





