YLR056W

2007-10-23T20:56:52Z

Rolfcraven: /* Community Commentary */

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004046 YLR056W]
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''ERG3 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''PSO6, SYR1''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XII:253862..254959
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004046
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'''Description of YLR056W:''' C-5 sterol desaturase, catalyzes the introduction of a C-5(6) double bond into episterol, a precursor in ergosterol biosynthesis; mutants are viable, but cannot grow on non-fermentable carbon sources<ref name='S000058496'>Paltauf F, et al. (1992) Regulation and compartmentalization of lipid synthesis in yeast. Pp. 415-500 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press {{SGDpaper|S000058496}} PMID </ref><ref name='S000042704'>Arthington BA, et al. (1991) Cloning, disruption and sequence of the gene encoding yeast C-5 sterol desaturase. Gene 102(1):39-44 {{SGDpaper|S000042704}} PMID 1864507</ref><ref name='S000039457'>Lees ND, et al. (1995) Cloning of the late genes in the ergosterol biosynthetic pathway of Saccharomyces cerevisiae--a review. Lipids 30(3):221-6 {{SGDpaper|S000039457}} PMID 7791529</ref><ref name='S000039432'>Parks LW, et al. (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30
{{SGDpaper|S000039432}} PMID 7791530</ref>
 
 
 
 
 
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==Community Commentary==
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Erg3 is activated by Dap1 (damage resistance protein 1), a heme-binding protein which shares some homology with cytochrome b5. Episterol accumulates in strains mutated for DAP1. Dap1p also activates Erg11, but dap1 strains engineered to over-express ERG11 have remarkable levels of episterol and other sterol intermediates. The mechanism through which Dap1p activates Erg3p is not known.




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==References==

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YPL170W

2007-10-23T15:11:09Z

Rolfcraven: /* Community Commentary */

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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?dbid=S000006091 YPL170W]
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''DAP1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XVI:228313..228771
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000006091
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'''Description of YPL170W:''' Heme-binding protein involved in regulation of cytochrome P450 protein Erg11p; damage response protein, related to mammalian membrane progesterone receptors; mutations lead to defects in telomeres, mitochondria, and sterol synthesis<ref name='S000080892'>Mallory JC, et al. (2005) Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae. Mol Cell Biol 25(5):1669-79 {{SGDpaper|S000080892}} PMID 15713626</ref><ref name='S000072913'>Hand RA, et al. (2003) Saccharomyces cerevisiae Dap1p, a novel DNA damage response protein related to the mammalian membrane-associated progesterone receptor. Eukaryot Cell 2(2):306-17
{{SGDpaper|S000072913}} PMID 12684380</ref>
 
 
 
 
 
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==Community Commentary==
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Dap1p is part of a widely conserved family of proteins that are structurally related to cytochrome b5. Dap1p is associated with damage resistance because cells lacking Dap1p are hyper-sensitive to the DNA damaging agent methyl methanesulfonate, and this function is conserved with its human homologue. Dap1p and its mouse, ''Schizosaccharomyces pombe'', and human homologues bind to heme, requiring highly conserved sequences in a region of the protein called the heme-1 domain. Dap1p binds to heme in a five-coordinate ferric state via a conserved tyrosine Y138 residue, while cytochrome b5 binds in a six-coordinate state via histidines. Dap1p functions by activating a cytochrome P450 protein called Erg11p (also called lanosterol demethylase or Cyp51p), which catalyzes a critical step of ergosterol synthesis. Erg11p is the target of the azole antifungal drugs, such as ketoconazole, fluconazole and miconazole, and Dap1p regulates the susceptibility of yeast cells to these drugs. Dap1p also activates Erg3p/ sterol C-5 desaturase, which is a proposed iron-binding protein, and Dap1p contributes to the uptake and intracellular transport of iron. The human homologue, called Hpr6 (human progesterone receptor/heme-1 domain protein) or PGRMC1 (progesterone receptor membrane component 1), is over-expressed in some types of human tumors and regulates damage sensitivity and sterol synthesis, suggesting conserved functions between the yeast and human homologues.




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YLR056W

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