Difference between revisions of "YLR364W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004356 YLR364W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004356 YLR364W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''GRX8 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''GRX8 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XII:854061..854390
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|nowrap| Chr XII:854062..854391
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004356
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004356
 
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'''Description of YLR364W:''' Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic<ref name='S000080191'>Haugen AC, et al. (2004) Integrating phenotypic and expression profiles to map arsenic-response networks. Genome Biol 5(12):R95 {{SGDpaper|S000080191}} PMID 15575969</ref><ref name='S000071347'>Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91 {{SGDpaper|S000071347}} PMID 12140549</ref><ref name='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 {{SGDpaper|S000074185}} PMID 14562095</ref><ref name='S000125083'>Mesecke N, et al. (2008) Two Novel Monothiol Glutaredoxins from Saccharomyces cerevisiae Provide Further Insight into Iron-Sulfur Cluster Binding, Oligomerization, and Enzymatic Activity of Glutaredoxins. Biochemistry 47(5):1452-63 {{SGDpaper|S000125083}} PMID 18171082</ref><ref name='S000129092'>Eckers E, et al. (2009) Biochemical Characterization of Dithiol Glutaredoxin 8 from Saccharomyces cerevisiae: The Catalytic Redox Mechanism Redux (dagger). Biochemistry
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'''Description of YLR364W:''' Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic<ref name='S000129092'>Eckers E, et al. (2009) Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux. Biochemistry 48(6):1410-23 {{SGDpaper|S000129092}} PMID 19166312</ref><ref name='S000071347'>Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91 {{SGDpaper|S000071347}} PMID 12140549</ref><ref name='S000080191'>Haugen AC, et al. (2004) Integrating phenotypic and expression profiles to map arsenic-response networks. Genome Biol 5(12):R95 {{SGDpaper|S000080191}} PMID 15575969</ref><ref name='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 {{SGDpaper|S000074185}} PMID 14562095</ref><ref name='S000125083'>Mesecke N, et al. (2008) Two Novel Monothiol Glutaredoxins from Saccharomyces cerevisiae Provide Further Insight into Iron-Sulfur Cluster Binding, Oligomerization, and Enzymatic Activity of Glutaredoxins. Biochemistry 47(5):1452-63
{{SGDpaper|S000129092}} PMID 19166312</ref>
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{{SGDpaper|S000125083}} PMID 18171082</ref>
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YLR364W
Gene name GRX8
Aliases
Feature type ORF, Verified
Coordinates Chr XII:854062..854391
Primary SGDID S000004356


Description of YLR364W: Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic[1][2][3][4][5]




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DNA and RNA Details

Other DNA and RNA Details

Other Topic: expression

Specifically higher expression in sulfur limited chemostat cultures versus sulfur excess. [6] [7]





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References

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  1. Eckers E, et al. (2009) Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux. Biochemistry 48(6):1410-23 SGD PMID 19166312
  2. Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91 SGD PMID 12140549
  3. Haugen AC, et al. (2004) Integrating phenotypic and expression profiles to map arsenic-response networks. Genome Biol 5(12):R95 SGD PMID 15575969
  4. Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
  5. Mesecke N, et al. (2008) Two Novel Monothiol Glutaredoxins from Saccharomyces cerevisiae Provide Further Insight into Iron-Sulfur Cluster Binding, Oligomerization, and Enzymatic Activity of Glutaredoxins. Biochemistry 47(5):1452-63 SGD PMID 18171082
  6. 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. J Biol Chem 278(5):3265-74 SGD PMID 12414795
  7. submitted by Viktor Boer on 2003-07-25

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