Difference between revisions of "YDR172W"
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| − | '''Description of YDR172W:''' Translation termination factor eRF3; altered protein conformation creates the [PSI(+)] prion, a dominant cytoplasmically inherited protein aggregate that alters translational fidelity and creates a nonsense suppressor phenotype<ref name=' | + | '''Description of YDR172W:''' Translation termination factor eRF3; altered protein conformation creates the [PSI(+)] prion, a dominant cytoplasmically inherited protein aggregate that alters translational fidelity and creates a nonsense suppressor phenotype<ref name='S000079184'>Lindquist S, et al. (2001) Investigating protein conformation-based inheritance and disease in yeast. Philos Trans R Soc Lond B Biol Sci 356(1406):169-76 {{SGDpaper|S000079184}} PMID 11260797</ref><ref name='S000079668'>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 {{SGDpaper|S000079668}} PMID 15326312</ref><ref name='S000080146'>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 |
| − | {{SGDpaper| | + | {{SGDpaper|S000080146}} PMID 15618222</ref> |
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Revision as of 03:15, 19 December 2008
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| Systematic name | YDR172W |
| Gene name | SUP35 |
| Aliases | GST1, PNM2, SAL3, SUF12, SUP2, SUP36, [PSI(+)], [PSI] |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:808322..810379 |
| Primary SGDID | S000002579 |
Description of YDR172W: Translation termination factor eRF3; altered protein conformation creates the [PSI(+)] prion, a dominant cytoplasmically inherited protein aggregate that alters translational fidelity and creates a nonsense suppressor phenotype[1][2][3]
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References
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- ↑ Lindquist S, et al. (2001) Investigating protein conformation-based inheritance and disease in yeast. Philos Trans R Soc Lond B Biol Sci 356(1406):169-76 SGD PMID 11260797
- ↑ 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 SGD PMID 15326312
- ↑ 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 SGD PMID 15618222
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