Difference between revisions of "YPL116W"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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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://www.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
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|nowrap| Chr XVI:329606..331699
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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='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='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='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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==Community Commentary==
 
==Community Commentary==
 
{{CommentaryHelp}}
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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<!--
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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Latest revision as of 07:45, 23 January 2012

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Systematic name YPL116W
Gene name HOS3
Aliases
Feature type ORF, Verified
Coordinates Chr XVI:329606..331699
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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Community Commentary

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References

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  1. 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
  2. Robyr D, et al. (2002) Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell 109(4):437-46 SGD PMID 12086601
  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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