Difference between revisions of "YDR172W"
SGDwikiBot (talk | contribs) (Automated import of articles) |
SGDwikiBot (talk | contribs) (Automated import of articles) |
||
| (10 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
<!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | ||
{{PageTop}} | {{PageTop}} | ||
| + | <protect> | ||
{|{{Prettytable}} align = 'right' width = '200px' | {|{{Prettytable}} align = 'right' width = '200px' | ||
|- | |- | ||
| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002579 YDR172W] |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SUP35 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SUP35 '' | ||
| Line 12: | Line 13: | ||
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr IV: | + | |nowrap| Chr IV:808324..810381 |
|- | |- | ||
| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002579 |
|} | |} | ||
<br> | <br> | ||
| − | '''Description of | + | '''Description of YDR172W:''' Translation termination factor eRF3, has a role in mRNA deadenylation and decay; altered protein conformation creates the [PSI(+)] prion that alters translational fidelity and results in a nonsense suppressor phenotype<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='S000136099'>Funakoshi Y, et al. (2007) Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes Dev 21(23):3135-48 {{SGDpaper|S000136099}} PMID 18056425</ref><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='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> |
<br> | <br> | ||
<br> | <br> | ||
<br> | <br> | ||
<br> | <br> | ||
| − | + | <br> | |
| + | </protect> | ||
__TOC__ | __TOC__ | ||
==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
| + | |||
| + | |||
| + | |||
| + | <!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation --> | ||
| + | <!-- | ||
| + | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
| + | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
| + | J Biol Chem 278(5):3265-74</ref> | ||
| + | --> | ||
| + | |||
| + | |||
| + | |||
| + | <protect> | ||
==References== | ==References== | ||
<!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | <!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | ||
{{RefHelp}} | {{RefHelp}} | ||
| + | </protect> | ||
Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YDR172W |
| Gene name | SUP35 |
| Aliases | GST1, PNM2, SAL3, SUF12, SUP2, SUP36, [PSI(+)], [PSI] |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:808324..810381 |
| Primary SGDID | S000002579 |
Description of YDR172W: Translation termination factor eRF3, has a role in mRNA deadenylation and decay; altered protein conformation creates the [PSI(+)] prion that alters translational fidelity and results in a nonsense suppressor phenotype[1][2][3][4]
</protect>
Contents
[hide]Community Commentary
About Community Commentary. Please share your knowledge!
<protect>
References
See Help:References on how to add references
- Jump up ↑ 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
- Jump up ↑ Funakoshi Y, et al. (2007) Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes Dev 21(23):3135-48 SGD PMID 18056425
- Jump up ↑ 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
- Jump up ↑ 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
See Help:Categories on how to add the wiki page for this gene to a Category </protect>
