Difference between revisions of "YMR313C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YMR313C YMR313C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004930 YMR313C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''TGL3 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''TGL3 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIII:901306..899378
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|nowrap| Chr XIII:901307..899379
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004930
 
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'''Description of {{PAGENAME}}:''' Triacylglycerol lipase of the lipid particle, responsible for all the TAG lipase activity of the lipid particle; contains the consensus sequence motif GXSXG, which is found in lipolytic enzymes<ref name='S000073557'>Athenstaedt K and Daum G (2003) YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae. J Biol Chem 278(26):23317-23
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'''Description of YMR313C:''' Bifunctional enzyme with triacylglycerol lipase and lysophosphatidylethanolamine acyltransferase activity; responsible for all the triacylglycerol lipase activity of the lipid particle; required with Tgl4p for timely bud formation<ref name='S000073557'>Athenstaedt K and Daum G (2003) YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae. J Biol Chem 278(26):23317-23 {{SGDpaper|S000073557}} PMID 12682047</ref><ref name='S000129072'>Kurat CF, et al. (2009) Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. Mol Cell 33(1):53-63 {{SGDpaper|S000129072}} PMID 19150427</ref><ref name='S000132735'>Rajakumari S and Daum G (2010) Janus-faced Enzymes Yeast Tgl3p and Tgl5p Catalyze Lipase and Acyltransferase Reactions. Mol Biol Cell 21(4):501-10
  {{SGDpaper|S000073557}} PMID 12682047</ref>
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  {{SGDpaper|S000132735}} PMID 20016004</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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=== Alleles, Strains, and Phenotypes ===
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[[Category:Topic:Alleles, Strains, and Phenotypes]]
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==== Multiple Knockout Strains ====
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[[Category:Topic:Alleles, Strains, and Phenotypes:Multiple Knockout Strains]]
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'''Together with''': TGL4<br>
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'''Phenotype(s)''': Loss of function (Null) [[Category:Phenotype:Loss of function (Null)]], Recessive [[Category:Phenotype:Recessive]], Viable [[Category:Phenotype:Viable]]
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tgl3 tgl4 double mutants are unable to degrade triglycerides in lag and early log-phases of growth <ref name='S000087074'>Kurat CF, et al. (2006) Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 281(1):491-500 {{SGDpaper|S000087074}} PMID 16267052</ref> <ref name = 'CAset3132-2006-05-22'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=3132 Sepp D. Kohlwein] on 2006-05-22</ref>
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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 07:45, 23 January 2012

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Systematic name YMR313C
Gene name TGL3
Aliases
Feature type ORF, Verified
Coordinates Chr XIII:901307..899379
Primary SGDID S000004930


Description of YMR313C: Bifunctional enzyme with triacylglycerol lipase and lysophosphatidylethanolamine acyltransferase activity; responsible for all the triacylglycerol lipase activity of the lipid particle; required with Tgl4p for timely bud formation[1][2][3]




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Community Commentary

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Alleles, Strains, and Phenotypes

Multiple Knockout Strains

Together with: TGL4
Phenotype(s): Loss of function (Null), Recessive, Viable

tgl3 tgl4 double mutants are unable to degrade triglycerides in lag and early log-phases of growth [4] [5]





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References

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  1. Athenstaedt K and Daum G (2003) YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae. J Biol Chem 278(26):23317-23 SGD PMID 12682047
  2. Kurat CF, et al. (2009) Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. Mol Cell 33(1):53-63 SGD PMID 19150427
  3. Rajakumari S and Daum G (2010) Janus-faced Enzymes Yeast Tgl3p and Tgl5p Catalyze Lipase and Acyltransferase Reactions. Mol Biol Cell 21(4):501-10 SGD PMID 20016004
  4. Kurat CF, et al. (2006) Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 281(1):491-500 SGD PMID 16267052
  5. submitted by Sepp D. Kohlwein on 2006-05-22

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