Difference between revisions of "YGR252W"

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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; founding member of the Gcn5p-related N-acetyltransferase superfamily<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='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='S000124028'>VanDemark AP, et al. (2007) Autoregulation of the rsc4 tandem bromodomain by gcn5 acetylation. Mol Cell 27(5):817-28
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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; founding member of the Gcn5p-related N-acetyltransferase superfamily; mutant displays reduced transcription elongation in the G-less-based run-on (GLRO) assay<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='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|S000124028}} PMID 17803945</ref>
 
  {{SGDpaper|S000124028}} PMID 17803945</ref>
 
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Revision as of 13:05, 15 August 2011

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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; founding member of the Gcn5p-related N-acetyltransferase superfamily; mutant displays reduced transcription elongation in the G-less-based run-on (GLRO) assay[1][2][3][4][5]




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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. Sterner DE and Berger SL (2000) Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64(2):435-59 SGD PMID 10839822
  4. 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
  5. 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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