Difference between revisions of "YGR252W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003484 YGR252W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003484 YGR252W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''GCN5 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''GCN5 ''
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''          ||''ADA4, SWI9''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''          ||''AAS104, ADA4, SWI9''
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''          || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''          || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr VII:996874..998193
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|nowrap| Chr VII:996869..998188
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003484
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003484
 
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'''Description of YGR252W:''' Histone acetyltransferase, acetylates N-terminal lysines on histones H2B and H3; catalytic subunit of the ADA and SAGA histone acetyltransferase complexes; founding member of the Gcn5p-related N-acetyltransferase superfamily<ref name='S000074512'>Langer MR, et al. (2001) Mutational analysis of conserved residues in the GCN5 family of histone acetyltransferases. J Biol Chem 276(33):31321-31 {{SGDpaper|S000074512}} PMID 11397810</ref><ref name='S000061032'>Sterner DE and Berger SL (2000) Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64(2):435-59
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'''Description of YGR252W:''' Acetyltransferase, modifies N-terminal lysines on histones H2B and H3; acetylates Rsc4p, a subunit of the RSC chromatin-remodeling complex, altering replication stress tolerance; catalytic subunit of the ADA and SAGA histone acetyltransferase complexes; mutant displays reduced transcription elongation in the G-less-based run-on (GLRO) assay; greater involvement in repression of RNAPII-dependent transcription than in activation<ref name='S000145695'>Charles GM, et al. (2011) Site-specific acetylation mark on an essential chromatin-remodeling complex promotes resistance to replication stress. Proc Natl Acad Sci U S A () {{SGDpaper|S000145695}} PMID 21673141</ref><ref name='S000074512'>Langer MR, et al. (2001) Mutational analysis of conserved residues in the GCN5 family of histone acetyltransferases. J Biol Chem 276(33):31321-31 {{SGDpaper|S000074512}} PMID 11397810</ref><ref name='S000150775'>Lanza AM, et al. (2012) Linking yeast Gcn5p catalytic function and gene regulation using a quantitative, graded dominant mutant approach. PLoS One 7(4):e36193 {{SGDpaper|S000150775}} PMID 22558379</ref><ref name='S000061032'>Sterner DE and Berger SL (2000) Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64(2):435-59 {{SGDpaper|S000061032}} PMID 10839822</ref><ref name='S000146226'>Tous C, et al. (2011) A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. EMBO J 30(10):1953-64 {{SGDpaper|S000146226}} PMID 21478823</ref><ref name='S000124028'>VanDemark AP, et al. (2007) Autoregulation of the rsc4 tandem bromodomain by gcn5 acetylation. Mol Cell 27(5):817-28
  {{SGDpaper|S000061032}} PMID 10839822</ref>
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  {{SGDpaper|S000124028}} PMID 17803945</ref>
 
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Latest revision as of 14:05, 11 September 2012

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Systematic name YGR252W
Gene name GCN5
Aliases AAS104, ADA4, SWI9
Feature type ORF, Verified
Coordinates Chr VII:996869..998188
Primary SGDID S000003484


Description of YGR252W: Acetyltransferase, modifies N-terminal lysines on histones H2B and H3; acetylates Rsc4p, a subunit of the RSC chromatin-remodeling complex, altering replication stress tolerance; catalytic subunit of the ADA and SAGA histone acetyltransferase complexes; mutant displays reduced transcription elongation in the G-less-based run-on (GLRO) assay; greater involvement in repression of RNAPII-dependent transcription than in activation[1][2][3][4][5][6]




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References

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  1. Charles GM, et al. (2011) Site-specific acetylation mark on an essential chromatin-remodeling complex promotes resistance to replication stress. Proc Natl Acad Sci U S A () SGD PMID 21673141
  2. Langer MR, et al. (2001) Mutational analysis of conserved residues in the GCN5 family of histone acetyltransferases. J Biol Chem 276(33):31321-31 SGD PMID 11397810
  3. Lanza AM, et al. (2012) Linking yeast Gcn5p catalytic function and gene regulation using a quantitative, graded dominant mutant approach. PLoS One 7(4):e36193 SGD PMID 22558379
  4. Sterner DE and Berger SL (2000) Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64(2):435-59 SGD PMID 10839822
  5. Tous C, et al. (2011) A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. EMBO J 30(10):1953-64 SGD PMID 21478823
  6. VanDemark AP, et al. (2007) Autoregulation of the rsc4 tandem bromodomain by gcn5 acetylation. Mol Cell 27(5):817-28 SGD PMID 17803945

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