YLL018C - Revision history

SGDwikiBot: Automated import of articles

2012-01-23T14:45:34Z

Automated import of articles

SGDwikiBot: Automated import of articles

2011-02-03T21:05:30Z

Automated import of articles

SGDwikiBot: Automated import of articles

2010-02-25T21:05:24Z

Automated import of articles

SGDwikiBot: Automated import of articles

2009-06-11T21:05:25Z

Automated import of articles

SGDwikiBot: Automated import of articles

2009-03-31T21:05:27Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-02-27T15:46:11Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-02-21T20:02:19Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-01-30T15:18:02Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-01-23T15:20:38Z

Automated import of articles

New page

{{PageTop}}
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YLL018C YLL018C]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''DPS1 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XII:111574..109901
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Cytoplasmic aspartyl-tRNA synthetase, homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation<ref name='S000076273'>Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83 {{SGDpaper|S000076273}} PMID 12888345</ref><ref name='S000062744'>Sauter C, et al. (2000) The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J Mol Biol 299(5):1313-24 {{SGDpaper|S000062744}} PMID 10873455</ref><ref name='S000062733'>Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 {{SGDpaper|S000062733}} PMID 3297688</ref><ref name='S000062732'>Lorber B, et al. (1988) Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain. Eur J Biochem 174(1):155-61 {{SGDpaper|S000062732}} PMID 3286258</ref><ref name='S000062722'>Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 {{SGDpaper|S000062722}} PMID 2047878</ref><ref name='S000056730'>Ruff M, et al. (1991) Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science 252(5013):1682-9 {{SGDpaper|S000056730}} PMID 2047877</ref><ref name='S000052929'>Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4
{{SGDpaper|S000052929}} PMID 8450889</ref>
 
 
 
 

__TOC__
==Community Commentary==
{{CommentaryHelp}}

==References==

{{RefHelp}}

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XII:111574..109901
+|nowrap| Chr XII:111575..109902
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000003941

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YLL018C:''' Aspartyl-tRNA synthetase, primarily cytoplasmic; homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation<ref name='S000052929'>Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4 {{SGDpaper|S000052929}} PMID 8450889</ref><ref name='S000056730'>Ruff M, et al. (1991) Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science 252(5013):1682-9 {{SGDpaper|S000056730}} PMID 2047877</ref><ref name='S000062722'>Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 {{SGDpaper|S000062722}} PMID 2047878</ref><ref name='S000062732'>Lorber B, et al. (1988) Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain. Eur J Biochem 174(1):155-61 {{SGDpaper|S000062732}} PMID 3286258</ref><ref name='S000062733'>Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 {{SGDpaper|S000062733}} PMID 3297688</ref><ref name='S000062744'>Sauter C, et al. (2000) The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J Mol Biol 299(5):1313-24 {{SGDpaper|S000062744}} PMID 10873455</ref><ref name='S000076273'>Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83
+'''Description of YLL018C:''' Aspartyl-tRNA synthetase, primarily cytoplasmic; homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation<ref name='S000052929'>Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4 {{SGDpaper|S000052929}} PMID 8450889</ref><ref name='S000076273'>Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83 {{SGDpaper|S000076273}} PMID 12888345</ref><ref name='S000062733'>Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 {{SGDpaper|S000062733}} PMID 3297688</ref><ref name='S000062732'>Lorber B, et al. (1988) Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain. Eur J Biochem 174(1):155-61 {{SGDpaper|S000062732}} PMID 3286258</ref><ref name='S000062722'>Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 {{SGDpaper|S000062722}} PMID 2047878</ref><ref name='S000056730'>Ruff M, et al. (1991) Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science 252(5013):1682-9 {{SGDpaper|S000056730}} PMID 2047877</ref><ref name='S000062744'>Sauter C, et al. (2000) The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J Mol Biol 299(5):1313-24
- {{SGDpaper|S000076273}} PMID 12888345</ref>
+ {{SGDpaper|S000062744}} PMID 10873455</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YLL018C:''' Cytoplasmic aspartyl-tRNA synthetase, homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation<ref name='S000052929'>Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4 {{SGDpaper|S000052929}} PMID 8450889</ref><ref name='S000056730'>Ruff M, et al. (1991) Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science 252(5013):1682-9 {{SGDpaper|S000056730}} PMID 2047877</ref><ref name='S000062722'>Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 {{SGDpaper|S000062722}} PMID 2047878</ref><ref name='S000062732'>Lorber B, et al. (1988) Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain. Eur J Biochem 174(1):155-61 {{SGDpaper|S000062732}} PMID 3286258</ref><ref name='S000062733'>Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 {{SGDpaper|S000062733}} PMID 3297688</ref><ref name='S000062744'>Sauter C, et al. (2000) The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J Mol Biol 299(5):1313-24 {{SGDpaper|S000062744}} PMID 10873455</ref><ref name='S000076273'>Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83
+'''Description of YLL018C:''' Aspartyl-tRNA synthetase, primarily cytoplasmic; homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation<ref name='S000052929'>Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4 {{SGDpaper|S000052929}} PMID 8450889</ref><ref name='S000056730'>Ruff M, et al. (1991) Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science 252(5013):1682-9 {{SGDpaper|S000056730}} PMID 2047877</ref><ref name='S000062722'>Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 {{SGDpaper|S000062722}} PMID 2047878</ref><ref name='S000062732'>Lorber B, et al. (1988) Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain. Eur J Biochem 174(1):155-61 {{SGDpaper|S000062732}} PMID 3286258</ref><ref name='S000062733'>Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 {{SGDpaper|S000062733}} PMID 3297688</ref><ref name='S000062744'>Sauter C, et al. (2000) The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J Mol Biol 299(5):1313-24 {{SGDpaper|S000062744}} PMID 10873455</ref><ref name='S000076273'>Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83
   {{SGDpaper|S000076273}} PMID 12888345</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YLL018C:''' Cytoplasmic aspartyl-tRNA synthetase, homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation<ref name='S000076273'>Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83 {{SGDpaper|S000076273}} PMID 12888345</ref><ref name='S000062744'>Sauter C, et al. (2000) The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J Mol Biol 299(5):1313-24 {{SGDpaper|S000062744}} PMID 10873455</ref><ref name='S000062733'>Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 {{SGDpaper|S000062733}} PMID 3297688</ref><ref name='S000062732'>Lorber B, et al. (1988) Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain. Eur J Biochem 174(1):155-61 {{SGDpaper|S000062732}} PMID 3286258</ref><ref name='S000062722'>Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 {{SGDpaper|S000062722}} PMID 2047878</ref><ref name='S000056730'>Ruff M, et al. (1991) Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science 252(5013):1682-9 {{SGDpaper|S000056730}} PMID 2047877</ref><ref name='S000052929'>Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4
+'''Description of YLL018C:''' Cytoplasmic aspartyl-tRNA synthetase, homodimeric enzyme that catalyzes the specific aspartylation of tRNA(Asp); class II aminoacyl tRNA synthetase; binding to its own mRNA may confer autoregulation<ref name='S000052929'>Cavarelli J, et al. (1993) Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362(6416):181-4 {{SGDpaper|S000052929}} PMID 8450889</ref><ref name='S000056730'>Ruff M, et al. (1991) Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science 252(5013):1682-9 {{SGDpaper|S000056730}} PMID 2047877</ref><ref name='S000062722'>Putz J, et al. (1991) Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase. Science 252(5013):1696-9 {{SGDpaper|S000062722}} PMID 2047878</ref><ref name='S000062732'>Lorber B, et al. (1988) Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain. Eur J Biochem 174(1):155-61 {{SGDpaper|S000062732}} PMID 3286258</ref><ref name='S000062733'>Lorber B, et al. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur J Biochem 165(2):409-17 {{SGDpaper|S000062733}} PMID 3297688</ref><ref name='S000062744'>Sauter C, et al. (2000) The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J Mol Biol 299(5):1313-24 {{SGDpaper|S000062744}} PMID 10873455</ref><ref name='S000076273'>Frugier M and Giege R (2003) Yeast aspartyl-tRNA synthetase binds specifically its own mRNA. J Mol Biol 331(2):375-83
-  {{SGDpaper|S000052929}} PMID 8450889</ref>
+  {{SGDpaper|S000076273}} PMID 12888345</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
Line 28:		Line 28:
	{{CommentaryHelp}}		{{CommentaryHelp}}

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

	<protect>		<protect>

@@ 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=S000003941 YLL018C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003941 YLL018C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''DPS1 ''

@@ Line 1: / Line 1: @@
 <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN-->
 {{PageTop}}
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
@@ Line 13: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XII:111574..109901
 |}
 <br>
@@ Line 23: / Line 22: @@
 <br>
 <br>
+<br>
 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}