Difference between revisions of "YLL002W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003925 YLL002W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RTT109 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RTT109 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XII: | + | |nowrap| Chr XII:146291..147601 |
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| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003925 |
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| − | '''Description of {{ | + | '''Description of YLL002W:''' Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p<ref name='S000120595'>Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 {{SGDpaper|S000120595}} PMID 17272722</ref><ref name='S000126328'>Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 {{SGDpaper|S000126328}} PMID 18458063</ref><ref name='S000120673'>Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 {{SGDpaper|S000120673}} PMID 17272723</ref><ref name='S000124825'>Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 {{SGDpaper|S000124825}} PMID 18036332</ref><ref name='S000068874'>Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65 |
{{SGDpaper|S000068874}} PMID 11779788</ref> | {{SGDpaper|S000068874}} PMID 11779788</ref> | ||
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==Community Commentary== | ==Community Commentary== | ||
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| + | 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> | ||
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==References== | ==References== | ||
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Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YLL002W |
| Gene name | RTT109 |
| Aliases | KIM2, REM50 |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:146291..147601 |
| Primary SGDID | S000003925 |
Description of YLL002W: Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p[1][2][3][4][5]
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Contents
Community Commentary
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References
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- ↑ Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52 SGD PMID 17272722
- ↑ Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53 SGD PMID 18458063
- ↑ Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5 SGD PMID 17272723
- ↑ Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64 SGD PMID 18036332
- ↑ Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65 SGD PMID 11779788
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