YER042W - 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=S000000844 YER042W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000844 YER042W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''MXR1 ''

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr V:234936..235490
+|nowrap| Chr V:234937..235491
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000000844

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YER042W:''' Methionine-S-sulfoxide reductase, involved in the response to oxidative stress; protects iron-sulfur clusters from oxidative inactivation along with MXR2; involved in the regulation of lifespan<ref name='S000043611'>Moskovitz J, et al. (1997) The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci U S A 94(18):9585-9 {{SGDpaper|S000043611}} PMID 9275166</ref><ref name='S000047290'>Moskovitz J, et al. (1998) Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci U S A 95(24):14071-5 {{SGDpaper|S000047290}} PMID 9826655</ref><ref name='S000076628'>Koc A, et al. (2004) Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging. Proc Natl Acad Sci U S A 101(21):7999-8004 {{SGDpaper|S000076628}} PMID 15141092</ref><ref name='S000069481'>Kryukov GV, et al. (2002) Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc Natl Acad Sci U S A 99(7):4245-50 {{SGDpaper|S000069481}} PMID 11929995</ref><ref name='S000128503'>Le DT, et al. (2009) Functional Analysis of Free Methionine-R-sulfoxide Reductase from Saccharomyces cerevisiae. J Biol Chem 284(7):4354-64 {{SGDpaper|S000128503}} PMID 19049972</ref><ref name='S000129314'>Sideri TC, et al. (2009) Methionine sulphoxide reductases protect iron-sulphur clusters from oxidative inactivation in yeast. Microbiology 155(Pt 2):612-23
+'''Description of YER042W:''' Methionine-S-sulfoxide reductase, involved in the response to oxidative stress; protects iron-sulfur clusters from oxidative inactivation along with MXR2; involved in the regulation of lifespan<ref name='S000076628'>Koc A, et al. (2004) Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging. Proc Natl Acad Sci U S A 101(21):7999-8004 {{SGDpaper|S000076628}} PMID 15141092</ref><ref name='S000069481'>Kryukov GV, et al. (2002) Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc Natl Acad Sci U S A 99(7):4245-50 {{SGDpaper|S000069481}} PMID 11929995</ref><ref name='S000128503'>Le DT, et al. (2009) Functional Analysis of Free Methionine-R-sulfoxide Reductase from Saccharomyces cerevisiae. J Biol Chem 284(7):4354-64 {{SGDpaper|S000128503}} PMID 19049972</ref><ref name='S000043611'>Moskovitz J, et al. (1997) The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci U S A 94(18):9585-9 {{SGDpaper|S000043611}} PMID 9275166</ref><ref name='S000047290'>Moskovitz J, et al. (1998) Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci U S A 95(24):14071-5 {{SGDpaper|S000047290}} PMID 9826655</ref><ref name='S000129314'>Sideri TC, et al. (2009) Methionine sulphoxide reductases protect iron-sulphur clusters from oxidative inactivation in yeast. Microbiology 155(Pt 2):612-23
   {{SGDpaper|S000129314}} PMID 19202110</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YER042W:''' Methionine-S-sulfoxide reductase, involved in the response to oxidative stress; protects iron-sulfur clusters from oxidative inactivation along with MXR2; involved in the regulation of lifespan<ref name='S000129314'>Sideri TC, et al. (2009) Methionine sulphoxide reductases protect iron-sulphur clusters from oxidative inactivation in yeast. Microbiology 155(Pt 2):612-23 {{SGDpaper|S000129314}} PMID 19202110</ref><ref name='S000128503'>Le DT, et al. (2009) Functional Analysis of Free Methionine-R-sulfoxide Reductase from Saccharomyces cerevisiae. J Biol Chem 284(7):4354-64 {{SGDpaper|S000128503}} PMID 19049972</ref><ref name='S000076628'>Koc A, et al. (2004) Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging. Proc Natl Acad Sci U S A 101(21):7999-8004 {{SGDpaper|S000076628}} PMID 15141092</ref><ref name='S000069481'>Kryukov GV, et al. (2002) Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc Natl Acad Sci U S A 99(7):4245-50 {{SGDpaper|S000069481}} PMID 11929995</ref><ref name='S000047290'>Moskovitz J, et al. (1998) Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci U S A 95(24):14071-5 {{SGDpaper|S000047290}} PMID 9826655</ref><ref name='S000043611'>Moskovitz J, et al. (1997) The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci U S A 94(18):9585-9
+'''Description of YER042W:''' Methionine-S-sulfoxide reductase, involved in the response to oxidative stress; protects iron-sulfur clusters from oxidative inactivation along with MXR2; involved in the regulation of lifespan<ref name='S000043611'>Moskovitz J, et al. (1997) The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci U S A 94(18):9585-9 {{SGDpaper|S000043611}} PMID 9275166</ref><ref name='S000047290'>Moskovitz J, et al. (1998) Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci U S A 95(24):14071-5 {{SGDpaper|S000047290}} PMID 9826655</ref><ref name='S000076628'>Koc A, et al. (2004) Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging. Proc Natl Acad Sci U S A 101(21):7999-8004 {{SGDpaper|S000076628}} PMID 15141092</ref><ref name='S000069481'>Kryukov GV, et al. (2002) Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc Natl Acad Sci U S A 99(7):4245-50 {{SGDpaper|S000069481}} PMID 11929995</ref><ref name='S000128503'>Le DT, et al. (2009) Functional Analysis of Free Methionine-R-sulfoxide Reductase from Saccharomyces cerevisiae. J Biol Chem 284(7):4354-64 {{SGDpaper|S000128503}} PMID 19049972</ref><ref name='S000129314'>Sideri TC, et al. (2009) Methionine sulphoxide reductases protect iron-sulphur clusters from oxidative inactivation in yeast. Microbiology 155(Pt 2):612-23
-  {{SGDpaper|S000043611}} PMID 9275166</ref>
+  {{SGDpaper|S000129314}} PMID 19202110</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YER042W:''' Peptide methionine sulfoxide reductase, reverses the oxidation of methionine residues; involved in oxidative damage repair, providing resistance to oxidative stress and regulation of lifespan<ref name='S000128503'>Le DT, et al. (2009) Functional Analysis of Free Methionine-R-sulfoxide Reductase from Saccharomyces cerevisiae. J Biol Chem 284(7):4354-64 {{SGDpaper|S000128503}} PMID 19049972</ref><ref name='S000073627'>Hanbauer I, et al. (2003) A homologue of elongation factor 1 gamma regulates methionine sulfoxide reductase A gene expression in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 100(14):8199-204 {{SGDpaper|S000073627}} PMID 12824466</ref><ref name='S000047290'>Moskovitz J, et al. (1998) Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci U S A 95(24):14071-5 {{SGDpaper|S000047290}} PMID 9826655</ref><ref name='S000043611'>Moskovitz J, et al. (1997) The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci U S A 94(18):9585-9
+'''Description of YER042W:''' Methionine-S-sulfoxide reductase, involved in the response to oxidative stress; protects iron-sulfur clusters from oxidative inactivation along with MXR2; involved in the regulation of lifespan<ref name='S000129314'>Sideri TC, et al. (2009) Methionine sulphoxide reductases protect iron-sulphur clusters from oxidative inactivation in yeast. Microbiology 155(Pt 2):612-23 {{SGDpaper|S000129314}} PMID 19202110</ref><ref name='S000128503'>Le DT, et al. (2009) Functional Analysis of Free Methionine-R-sulfoxide Reductase from Saccharomyces cerevisiae. J Biol Chem 284(7):4354-64 {{SGDpaper|S000128503}} PMID 19049972</ref><ref name='S000076628'>Koc A, et al. (2004) Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging. Proc Natl Acad Sci U S A 101(21):7999-8004 {{SGDpaper|S000076628}} PMID 15141092</ref><ref name='S000069481'>Kryukov GV, et al. (2002) Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc Natl Acad Sci U S A 99(7):4245-50 {{SGDpaper|S000069481}} PMID 11929995</ref><ref name='S000047290'>Moskovitz J, et al. (1998) Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci U S A 95(24):14071-5 {{SGDpaper|S000047290}} PMID 9826655</ref><ref name='S000043611'>Moskovitz J, et al. (1997) The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci U S A 94(18):9585-9
   {{SGDpaper|S000043611}} PMID 9275166</ref>
 <br>

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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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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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