YNL229C
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| Systematic name | YNL229C |
| Gene name | URE2 |
| Aliases | [URE3] |
| Feature type | ORF, Verified |
| Coordinates | Chr XIV:220202..219138 |
| Primary SGDID | S000005173 |
Description of YNL229C: Nitrogen catabolite repression transcriptional regulator that acts by inhibition of GLN3 transcription in good nitrogen source; has glutathione peroxidase activity and can mutate to acquire GST activity; altered form creates [URE3] prion[1][2][3][4][5]
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Community Commentary
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The Ure2 protein is composed of 354 amino acids, which compose two distinct domains. The amino-terminal sequence (~90 residues) forms the prion domain, which contains the necessary amino acids for the formation and propagation of the prion form of Ure2p. The c-terminal region of Ure2p is the Nitrogen Catabolite Repression (NCR) domain, which is required for repression of genes involved in nitrogen catabolism. Dispensing with the prion domain disables the capacity of Ure2p to form a prion.
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References
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- ↑ Zhang ZR, et al. (2008) Restoration of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2. J Mol Biol 384(3):641-51 SGD PMID 18845158
- ↑ Bai M, et al. (2004) The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J Biol Chem 279(48):50025-30 SGD PMID 15371425
- ↑ Wickner RB (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264(5158):566-9 SGD PMID 7909170
- ↑ Blinder D, et al. (1996) Interaction of the GATA factor Gln3p with the nitrogen regulator Ure2p in Saccharomyces cerevisiae. J Bacteriol 178(15):4734-6 SGD PMID 8755910
- ↑ Courchesne WE and Magasanik B (1988) Regulation of nitrogen assimilation in Saccharomyces cerevisiae: roles of the URE2 and GLN3 genes. J Bacteriol 170(2):708-13 SGD PMID 2892826
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References
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