Difference between revisions of "YPL116W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YPL116W YPL116W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006037 YPL116W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HOS3 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HOS3 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|nowrap| Chr XVI:329605..331698
 
|nowrap| Chr XVI:329605..331698
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000006037
 
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'''Description of {{PAGENAME}}:''' Trichostatin A-insensitive homodimeric histone deacetylase (HDAC) with specificity in vitro for histones H3, H4, H2A, and H2B; similar to Hda1p, Rpd3p, Hos1p, and Hos2p; deletion results in increased histone acetylation at rDNA repeats<ref name='S000070188'>Robyr D, et al. (2002) Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 109(4):437-46 {{SGDpaper|S000070188}} PMID 12086601</ref><ref name='S000055221'>Carmen AA, et al. (1999) Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity. Proc Natl Acad Sci U S A 96(22):12356-61 {{SGDpaper|S000055221}} PMID 10535926</ref><ref name='S000047708'>Rundlett SE, et al. (1996) HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci U S A 93(25):14503-8
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'''Description of YPL116W:''' Trichostatin A-insensitive homodimeric histone deacetylase (HDAC) with specificity in vitro for histones H3, H4, H2A, and H2B; similar to Hda1p, Rpd3p, Hos1p, and Hos2p; deletion results in increased histone acetylation at rDNA repeats<ref name='S000070188'>Robyr D, et al. (2002) Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 109(4):437-46 {{SGDpaper|S000070188}} PMID 12086601</ref><ref name='S000055221'>Carmen AA, et al. (1999) Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity. Proc Natl Acad Sci U S A 96(22):12356-61 {{SGDpaper|S000055221}} PMID 10535926</ref><ref name='S000047708'>Rundlett SE, et al. (1996) HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci U S A 93(25):14503-8
 
  {{SGDpaper|S000047708}} PMID 8962081</ref>
 
  {{SGDpaper|S000047708}} PMID 8962081</ref>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Revision as of 08:46, 27 February 2007

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Systematic name YPL116W
Gene name HOS3
Aliases
Feature type ORF, Verified
Coordinates Chr XVI:329605..331698
Primary SGDID S000006037


Description of YPL116W: Trichostatin A-insensitive homodimeric histone deacetylase (HDAC) with specificity in vitro for histones H3, H4, H2A, and H2B; similar to Hda1p, Rpd3p, Hos1p, and Hos2p; deletion results in increased histone acetylation at rDNA repeats[1][2][3]




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References

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  1. Robyr D, et al. (2002) Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 109(4):437-46 SGD PMID 12086601
  2. Carmen AA, et al. (1999) Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity. Proc Natl Acad Sci U S A 96(22):12356-61 SGD PMID 10535926
  3. Rundlett SE, et al. (1996) HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci U S A 93(25):14503-8 SGD PMID 8962081

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