Difference between revisions of "YOR202W"
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− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005728 YOR202W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HIS3 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HIS3 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XV:721947..722609 | |nowrap| Chr XV:721947..722609 | ||
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+ | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005728 | ||
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<br> | <br> | ||
− | '''Description of | + | '''Description of YOR202W:''' Imidazoleglycerol-phosphate dehydratase, catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p<ref name='S000057959'>Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 {{SGDpaper|S000057959}} PMID 8852895</ref><ref name='S000053704'>Pearce DA and Sherman F (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9 {{SGDpaper|S000053704}} PMID 10438744</ref><ref name='S000051610'>Hope IA and Struhl K (1985) GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. Cell 43(1):177-88 {{SGDpaper|S000051610}} PMID 3907851</ref><ref name='S000048780'>Struhl K and Davis RW (1977) Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazole-glycerolphosphate dehydratase (his3). Proc Natl Acad Sci U S A 74(12):5255-9 |
{{SGDpaper|S000048780}} PMID 341150</ref> | {{SGDpaper|S000048780}} PMID 341150</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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<protect> | <protect> |
Revision as of 08:46, 27 February 2007
Share your knowledge...Edit this entry! <protect>
Systematic name | YOR202W |
Gene name | HIS3 |
Aliases | HIS10 |
Feature type | ORF, Verified |
Coordinates | Chr XV:721947..722609 |
Primary SGDID | S000005728 |
Description of YOR202W: Imidazoleglycerol-phosphate dehydratase, catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p[1][2][3][4]
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References
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- ↑ Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69 SGD PMID 8852895
- ↑ Pearce DA and Sherman F (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9 SGD PMID 10438744
- ↑ Hope IA and Struhl K (1985) GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. Cell 43(1):177-88 SGD PMID 3907851
- ↑ Struhl K and Davis RW (1977) Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazole-glycerolphosphate dehydratase (his3). Proc Natl Acad Sci U S A 74(12):5255-9 SGD PMID 341150
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