Difference between revisions of "YNL072W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YNL072W YNL072W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005016 YNL072W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RNH201 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RNH201 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIV:490318..491241
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|nowrap| Chr XIV:490317..491240
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005016
 
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'''Description of {{PAGENAME}}:''' Ribonuclease H2 catalytic subunit, removes RNA primers during Okazaki fragment synthesis; cooperates with Rad27p nuclease<ref name='S000050269'>Frank P, et al. (1998) Yeast RNase H(35) is the counterpart of the mammalian RNase HI, and is evolutionarily related to prokaryotic RNase HII. FEBS Lett 421(1):23-6 {{SGDpaper|S000050269}} PMID 9462832</ref><ref name='S000048942'>Qiu J, et al. (1999) Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease. Mol Cell Biol 19(12):8361-71
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'''Description of YNL072W:''' Ribonuclease H2 catalytic subunit, removes RNA primers during Okazaki fragment synthesis and errant ribonucleotides misincorporated during DNA replication; homolog of RNAse HI; related to human AGS4 which causes Aicardi-Goutieres syndrome<ref name='S000128478'>Crow YJ, et al. (2006) Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutieres syndrome and mimic congenital viral brain infection. Nat Genet 38(8):910-6 {{SGDpaper|S000128478}} PMID 16845400</ref><ref name='S000050269'>Frank P, et al. (1998) Yeast RNase H(35) is the counterpart of the mammalian RNase HI, and is evolutionarily related to prokaryotic RNase HII. FEBS Lett 421(1):23-6 {{SGDpaper|S000050269}} PMID 9462832</ref><ref name='S000136054'>Nick McElhinny SA, et al. (2010) Genome instability due to ribonucleotide incorporation into DNA. Nat Chem Biol 6(10):774-81 {{SGDpaper|S000136054}} PMID 20729855</ref><ref name='S000048942'>Qiu J, et al. (1999) Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease. Mol Cell Biol 19(12):8361-71
 
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==Community Commentary==
 
==Community Commentary==
 
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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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==References==
 
==References==
 
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Latest revision as of 06:45, 23 January 2012

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Systematic name YNL072W
Gene name RNH201
Aliases RNH35
Feature type ORF, Verified
Coordinates Chr XIV:490317..491240
Primary SGDID S000005016


Description of YNL072W: Ribonuclease H2 catalytic subunit, removes RNA primers during Okazaki fragment synthesis and errant ribonucleotides misincorporated during DNA replication; homolog of RNAse HI; related to human AGS4 which causes Aicardi-Goutieres syndrome[1][2][3][4]




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References

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  1. Crow YJ, et al. (2006) Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutieres syndrome and mimic congenital viral brain infection. Nat Genet 38(8):910-6 SGD PMID 16845400
  2. Frank P, et al. (1998) Yeast RNase H(35) is the counterpart of the mammalian RNase HI, and is evolutionarily related to prokaryotic RNase HII. FEBS Lett 421(1):23-6 SGD PMID 9462832
  3. Nick McElhinny SA, et al. (2010) Genome instability due to ribonucleotide incorporation into DNA. Nat Chem Biol 6(10):774-81 SGD PMID 20729855
  4. Qiu J, et al. (1999) Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease. Mol Cell Biol 19(12):8361-71 SGD PMID 10567561

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