Difference between revisions of "YER049W"
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| − | '''Description of YER049W:''' | + | '''Description of YER049W:''' Poly(rA)-binding protein involved in translation termination efficiency, mRNA poly(A) tail length and mRNA stability; interacts with Sup45p (eRF1), Sup35p (eRF3) and Pab1p; similar to prolyl 4-hydroxylases; binds Fe(III) and 2-oxoglutarate<ref name='S000116842'>Keeling KM, et al. (2006) Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae. Mol Cell Biol 26(14):5237-48 {{SGDpaper|S000116842}} PMID 16809762</ref><ref name='S000132569'>Kim HS, et al. (2009) Crystal structure of Tpa1 from Saccharomyces cerevisiae, a component of the messenger ribonucleoprotein complex. Nucleic Acids Res () |
| − | {{SGDpaper| | + | {{SGDpaper|S000132569}} PMID 20040577</ref> |
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Revision as of 14:05, 4 January 2010
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| Systematic name | YER049W |
| Gene name | TPA1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr V:251727..253661 |
| Primary SGDID | S000000851 |
Description of YER049W: Poly(rA)-binding protein involved in translation termination efficiency, mRNA poly(A) tail length and mRNA stability; interacts with Sup45p (eRF1), Sup35p (eRF3) and Pab1p; similar to prolyl 4-hydroxylases; binds Fe(III) and 2-oxoglutarate[1][2]
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Contents
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References
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- ↑ Keeling KM, et al. (2006) Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae. Mol Cell Biol 26(14):5237-48 SGD PMID 16809762
- ↑ Kim HS, et al. (2009) Crystal structure of Tpa1 from Saccharomyces cerevisiae, a component of the messenger ribonucleoprotein complex. Nucleic Acids Res () SGD PMID 20040577
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