Difference between revisions of "YBL005W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YBL005W YBL005W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000101 YBL005W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PDR3 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PDR3 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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|nowrap| Chr II:217473..220403
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|nowrap| Chr II:217470..220400
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000101
 
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'''Description of {{PAGENAME}}:''' Transcriptional activator of the pleiotropic drug resistance network, regulates expression of ATP-binding cassette (ABC) transporters through binding to cis-acting sites known as PDREs (PDR responsive elements)<ref name='S000056021'>Kean LS, et al. (1997) Plasma membrane translocation of fluorescent-labeled phosphatidylethanolamine is controlled by transcription regulators, PDR1 and PDR3. J Cell Biol 138(2):255-70 {{SGDpaper|S000056021}} PMID 9230069</ref><ref name='S000055982'>Balzi E and Goffeau A (1995) Yeast multidrug resistance: the PDR network. J Bioenerg Biomembr 27(1):71-6 {{SGDpaper|S000055982}} PMID 7629054</ref><ref name='S000048471'>Delaveau T, et al. (1994) PDR3, a new yeast regulatory gene, is homologous to PDR1 and controls the multidrug resistance phenomenon. Mol Gen Genet 244(5):501-11 {{SGDpaper|S000048471}} PMID 8078477</ref><ref name='S000046396'>Wolfger H, et al. (1997) The yeast ATP binding cassette (ABC) protein genes PDR10 and PDR15 are novel targets for the Pdr1 and Pdr3 transcriptional regulators. FEBS Lett 418(3):269-74
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'''Description of YBL005W:''' Transcriptional activator of the pleiotropic drug resistance network; regulates expression of ATP-binding cassette (ABC) transporters through binding to cis-acting sites known as PDREs (PDR responsive elements); post-translationally up-regulated in cells lacking a functional mitochondrial genome; PDR3 has a paralog, PDR1, that arose from the whole genome duplication<ref name='S000055982'>Balzi E and Goffeau A (1995) Yeast multidrug resistance: the PDR network. J Bioenerg Biomembr 27(1):71-6 {{SGDpaper|S000055982}} PMID 7629054</ref><ref name='S000113653'>Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 {{SGDpaper|S000113653}} PMID 16169922</ref><ref name='S000048471'>Delaveau T, et al. (1994) PDR3, a new yeast regulatory gene, is homologous to PDR1 and controls the multidrug resistance phenomenon. Mol Gen Genet 244(5):501-11 {{SGDpaper|S000048471}} PMID 8078477</ref><ref name='S000069828'>Devaux F, et al. (2002) Genome-wide studies on the nuclear PDR3-controlled response to mitochondrial dysfunction in yeast. FEBS Lett 515(1-3):25-8 {{SGDpaper|S000069828}} PMID 11943188</ref><ref name='S000056021'>Kean LS, et al. (1997) Plasma membrane translocation of fluorescent-labeled phosphatidylethanolamine is controlled by transcription regulators, PDR1 and PDR3. J Cell Biol 138(2):255-70 {{SGDpaper|S000056021}} PMID 9230069</ref><ref name='S000046396'>Wolfger H, et al. (1997) The yeast ATP binding cassette (ABC) protein genes PDR10 and PDR15 are novel targets for the Pdr1 and Pdr3 transcriptional regulators. FEBS Lett 418(3):269-74 {{SGDpaper|S000046396}} PMID 9428726</ref><ref name='S000068775'>Zhang X and Moye-Rowley WS (2001) Saccharomyces cerevisiae multidrug resistance gene expression inversely correlates with the status of the F(0) component of the mitochondrial ATPase. J Biol Chem 276(51):47844-52
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  {{SGDpaper|S000068775}} PMID 11602584</ref>
 
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==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 13:05, 31 August 2012

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Systematic name YBL005W
Gene name PDR3
Aliases AMY2, TPE2
Feature type ORF, Verified
Coordinates Chr II:217470..220400
Primary SGDID S000000101


Description of YBL005W: Transcriptional activator of the pleiotropic drug resistance network; regulates expression of ATP-binding cassette (ABC) transporters through binding to cis-acting sites known as PDREs (PDR responsive elements); post-translationally up-regulated in cells lacking a functional mitochondrial genome; PDR3 has a paralog, PDR1, that arose from the whole genome duplication[1][2][3][4][5][6][7]




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Community Commentary

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References

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  1. ↑ Balzi E and Goffeau A (1995) Yeast multidrug resistance: the PDR network. J Bioenerg Biomembr 27(1):71-6 SGD PMID 7629054
  2. ↑ Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 SGD PMID 16169922
  3. ↑ Delaveau T, et al. (1994) PDR3, a new yeast regulatory gene, is homologous to PDR1 and controls the multidrug resistance phenomenon. Mol Gen Genet 244(5):501-11 SGD PMID 8078477
  4. ↑ Devaux F, et al. (2002) Genome-wide studies on the nuclear PDR3-controlled response to mitochondrial dysfunction in yeast. FEBS Lett 515(1-3):25-8 SGD PMID 11943188
  5. ↑ Kean LS, et al. (1997) Plasma membrane translocation of fluorescent-labeled phosphatidylethanolamine is controlled by transcription regulators, PDR1 and PDR3. J Cell Biol 138(2):255-70 SGD PMID 9230069
  6. ↑ Wolfger H, et al. (1997) The yeast ATP binding cassette (ABC) protein genes PDR10 and PDR15 are novel targets for the Pdr1 and Pdr3 transcriptional regulators. FEBS Lett 418(3):269-74 SGD PMID 9428726
  7. ↑ Zhang X and Moye-Rowley WS (2001) Saccharomyces cerevisiae multidrug resistance gene expression inversely correlates with the status of the F(0) component of the mitochondrial ATPase. J Biol Chem 276(51):47844-52 SGD PMID 11602584

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