YDR232W - Revision history

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002640 YDR232W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002640 YDR232W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''HEM1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr IV:927449..929095
+|nowrap| Chr IV:927452..929098
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000002640

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR232W:''' 5-aminolevulinate synthase, catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p<ref name='S000045140'>Keng T and Guarente L (1987) Constitutive expression of the yeast HEM1 gene is actually a composite of activation and repression. Proc Natl Acad Sci U S A 84(24):9113-7 {{SGDpaper|S000045140}} PMID 3321068</ref><ref name='S000046021'>Gollub EG, et al. (1977) Yeast mutants deficient in heme biosynthesis and a heme mutant additionally blocked in cyclization of 2,3-oxidosqualene. J Biol Chem 252(9):2846-54 {{SGDpaper|S000046021}} PMID 323256</ref><ref name='S000047507'>Urban-Grimal D, et al. (1986) The nucleotide sequence of the HEM1 gene and evidence for a precursor form of the mitochondrial 5-aminolevulinate synthase in Saccharomyces cerevisiae. Eur J Biochem 156(3):511-9 {{SGDpaper|S000047507}} PMID 3516694</ref><ref name='S000054004'>Keng T, et al. (1986) The nine amino-terminal residues of delta-aminolevulinate synthase direct beta-galactosidase into the mitochondrial matrix. Mol Cell Biol 6(2):355-64 {{SGDpaper|S000054004}} PMID 3023841</ref><ref name='S000054307'>Haldi M and Guarente L (1989) N-terminal deletions of a mitochondrial signal sequence in yeast. Targeting information of delta-aminolevulinate synthase is encoded in non-overlapping regions. J Biol Chem 264(29):17107-12 {{SGDpaper|S000054307}} PMID 2507539</ref><ref name='S000057328'>Urban-Grimal D and Labbe-Bois R (1981) Genetic and biochemical characterization of mutants of Saccharomyces cerevisiae blocked in six different steps of heme biosynthesis. Mol Gen Genet 183(1):85-92
+'''Description of YDR232W:''' 5-aminolevulinate synthase, catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p<ref name='S000046021'>Gollub EG, et al. (1977) Yeast mutants deficient in heme biosynthesis and a heme mutant additionally blocked in cyclization of 2,3-oxidosqualene. J Biol Chem 252(9):2846-54 {{SGDpaper|S000046021}} PMID 323256</ref><ref name='S000054307'>Haldi M and Guarente L (1989) N-terminal deletions of a mitochondrial signal sequence in yeast. Targeting information of delta-aminolevulinate synthase is encoded in non-overlapping regions. J Biol Chem 264(29):17107-12 {{SGDpaper|S000054307}} PMID 2507539</ref><ref name='S000045140'>Keng T and Guarente L (1987) Constitutive expression of the yeast HEM1 gene is actually a composite of activation and repression. Proc Natl Acad Sci U S A 84(24):9113-7 {{SGDpaper|S000045140}} PMID 3321068</ref><ref name='S000054004'>Keng T, et al. (1986) The nine amino-terminal residues of delta-aminolevulinate synthase direct beta-galactosidase into the mitochondrial matrix. Mol Cell Biol 6(2):355-64 {{SGDpaper|S000054004}} PMID 3023841</ref><ref name='S000057328'>Urban-Grimal D and Labbe-Bois R (1981) Genetic and biochemical characterization of mutants of Saccharomyces cerevisiae blocked in six different steps of heme biosynthesis. Mol Gen Genet 183(1):85-92 {{SGDpaper|S000057328}} PMID 7035824</ref><ref name='S000047507'>Urban-Grimal D, et al. (1986) The nucleotide sequence of the HEM1 gene and evidence for a precursor form of the mitochondrial 5-aminolevulinate synthase in Saccharomyces cerevisiae. Eur J Biochem 156(3):511-9
-  {{SGDpaper|S000057328}} PMID 7035824</ref>
+  {{SGDpaper|S000047507}} PMID 3516694</ref>
 <br>
 <br>

@@ Line 8: / Line 8: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''HEM1 ''
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||''CYD1''
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||''CYD1, OLE3''
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''           || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR232W:''' 5-aminolevulinate synthase, catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p<ref name='S000057328'>Urban-Grimal D and Labbe-Bois R (1981) Genetic and biochemical characterization of mutants of Saccharomyces cerevisiae blocked in six different steps of heme biosynthesis. Mol Gen Genet 183(1):85-92 {{SGDpaper|S000057328}} PMID 7035824</ref><ref name='S000054307'>Haldi M and Guarente L (1989) N-terminal deletions of a mitochondrial signal sequence in yeast. Targeting information of delta-aminolevulinate synthase is encoded in non-overlapping regions. J Biol Chem 264(29):17107-12 {{SGDpaper|S000054307}} PMID 2507539</ref><ref name='S000054004'>Keng T, et al. (1986) The nine amino-terminal residues of delta-aminolevulinate synthase direct beta-galactosidase into the mitochondrial matrix. Mol Cell Biol 6(2):355-64 {{SGDpaper|S000054004}} PMID 3023841</ref><ref name='S000047507'>Urban-Grimal D, et al. (1986) The nucleotide sequence of the HEM1 gene and evidence for a precursor form of the mitochondrial 5-aminolevulinate synthase in Saccharomyces cerevisiae. Eur J Biochem 156(3):511-9 {{SGDpaper|S000047507}} PMID 3516694</ref><ref name='S000046021'>Gollub EG, et al. (1977) Yeast mutants deficient in heme biosynthesis and a heme mutant additionally blocked in cyclization of 2,3-oxidosqualene. J Biol Chem 252(9):2846-54 {{SGDpaper|S000046021}} PMID 323256</ref><ref name='S000045140'>Keng T and Guarente L (1987) Constitutive expression of the yeast HEM1 gene is actually a composite of activation and repression. Proc Natl Acad Sci U S A 84(24):9113-7
+'''Description of YDR232W:''' 5-aminolevulinate synthase, catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p<ref name='S000045140'>Keng T and Guarente L (1987) Constitutive expression of the yeast HEM1 gene is actually a composite of activation and repression. Proc Natl Acad Sci U S A 84(24):9113-7 {{SGDpaper|S000045140}} PMID 3321068</ref><ref name='S000046021'>Gollub EG, et al. (1977) Yeast mutants deficient in heme biosynthesis and a heme mutant additionally blocked in cyclization of 2,3-oxidosqualene. J Biol Chem 252(9):2846-54 {{SGDpaper|S000046021}} PMID 323256</ref><ref name='S000047507'>Urban-Grimal D, et al. (1986) The nucleotide sequence of the HEM1 gene and evidence for a precursor form of the mitochondrial 5-aminolevulinate synthase in Saccharomyces cerevisiae. Eur J Biochem 156(3):511-9 {{SGDpaper|S000047507}} PMID 3516694</ref><ref name='S000054004'>Keng T, et al. (1986) The nine amino-terminal residues of delta-aminolevulinate synthase direct beta-galactosidase into the mitochondrial matrix. Mol Cell Biol 6(2):355-64 {{SGDpaper|S000054004}} PMID 3023841</ref><ref name='S000054307'>Haldi M and Guarente L (1989) N-terminal deletions of a mitochondrial signal sequence in yeast. Targeting information of delta-aminolevulinate synthase is encoded in non-overlapping regions. J Biol Chem 264(29):17107-12 {{SGDpaper|S000054307}} PMID 2507539</ref><ref name='S000057328'>Urban-Grimal D and Labbe-Bois R (1981) Genetic and biochemical characterization of mutants of Saccharomyces cerevisiae blocked in six different steps of heme biosynthesis. Mol Gen Genet 183(1):85-92
-  {{SGDpaper|S000045140}} PMID 3321068</ref>
+  {{SGDpaper|S000057328}} PMID 7035824</ref>
 <br>
 <br>

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		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<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.
		+	J Biol Chem 278(5):3265-74</ref>
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