YBL071W-A - Revision history

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{{PageTop}}
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YBL071W-A YBL071W-A]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''KTI11 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''DPH3''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr II:89976..90224
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Protein required for synthesis of diphthamide, a modified histidine residue of translation elongation factor 2; functions with Dph1p, Dph2p, Jjj3p, and Dph5p; required, with Elongator complex, for modification of wobble nucleosides in tRNA<ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75
{{SGDpaper|S000069896}} PMID 11994165</ref>
 
 
 
 

__TOC__
==Community Commentary==
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==References==

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@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr II:89976..90224
+|nowrap| Chr II:89978..90226
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000007587

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBL071W-A:''' Zn-ribbon protein that co-purifies with Dph1 and Dph2 in a complex required for synthesis of diphthamide on translation factor eEF2 and with Elongator subunits Iki3p, Elp2p, and Elp3p involved in modification of wobble nucleosides in tRNAs<ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75 {{SGDpaper|S000069896}} PMID 11994165</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000124746'>Proudfoot M, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375(1):301-15 {{SGDpaper|S000124746}} PMID 18021800</ref><ref name='S000127043'>Bar C, et al. (2008) A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3. Mol Microbiol 69(5):1221-33
+'''Description of YBL071W-A:''' Zn-ribbon protein that co-purifies with Dph1 and Dph2 in a complex required for synthesis of diphthamide on translation factor eEF2 and with Elongator subunits Iki3p, Elp2p, and Elp3p involved in modification of wobble nucleosides in tRNAs<ref name='S000127043'>Bar C, et al. (2008) A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3. Mol Microbiol 69(5):1221-33 {{SGDpaper|S000127043}} PMID 18627462</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75 {{SGDpaper|S000069896}} PMID 11994165</ref><ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000124746'>Proudfoot M, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375(1):301-15
- {{SGDpaper|S000127043}} PMID 18627462</ref>
+ {{SGDpaper|S000124746}} PMID 18021800</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBL071W-A:''' Zn-ribbon protein that co-purifies with Dph1, Dph2, Eft2 and Elongator subunits Iki3p, Elp2p, and Elp3p as a complex required for synthesis of diphthamide, a modified histidine residue, and for modification of wobble nucleosides in tRNA<ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75 {{SGDpaper|S000069896}} PMID 11994165</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000124746'>Proudfoot M, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375(1):301-15
+'''Description of YBL071W-A:''' Zn-ribbon protein that co-purifies with Dph1 and Dph2 in a complex required for synthesis of diphthamide on translation factor eEF2 and with Elongator subunits Iki3p, Elp2p, and Elp3p involved in modification of wobble nucleosides in tRNAs<ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75 {{SGDpaper|S000069896}} PMID 11994165</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000124746'>Proudfoot M, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375(1):301-15 {{SGDpaper|S000124746}} PMID 18021800</ref><ref name='S000127043'>Bar C, et al. (2008) A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3. Mol Microbiol 69(5):1221-33
-  {{SGDpaper|S000124746}} PMID 18021800</ref>
+  {{SGDpaper|S000127043}} PMID 18627462</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBL071W-A:''' Zn-ribbon protein that co-purifies with Dph1, Dph2, Eft2 and Elongator subunits Iki3p, Elp2p, and Elp3p as a complex required for synthesis of diphthamide, a modified histidine residue, and for modification of wobble nucleosides in tRNA<ref name='S000124746'>Proudfoot M, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375(1):301-15 {{SGDpaper|S000124746}} PMID 18021800</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75
+'''Description of YBL071W-A:''' Zn-ribbon protein that co-purifies with Dph1, Dph2, Eft2 and Elongator subunits Iki3p, Elp2p, and Elp3p as a complex required for synthesis of diphthamide, a modified histidine residue, and for modification of wobble nucleosides in tRNA<ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75 {{SGDpaper|S000069896}} PMID 11994165</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000124746'>Proudfoot M, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375(1):301-15
-  {{SGDpaper|S000069896}} PMID 11994165</ref>
+  {{SGDpaper|S000124746}} PMID 18021800</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YBL071W-A:''' Protein required for synthesis of diphthamide, a modified histidine residue of translation elongation factor 2; functions with Dph1p, Dph2p, Jjj3p, and Dph5p; required, with Elongator complex, for modification of wobble nucleosides in tRNA<ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75
+'''Description of YBL071W-A:''' Zn-ribbon protein that co-purifies with Dph1, Dph2, Eft2 and Elongator subunits Iki3p, Elp2p, and Elp3p as a complex required for synthesis of diphthamide, a modified histidine residue, and for modification of wobble nucleosides in tRNA<ref name='S000124746'>Proudfoot M, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375(1):301-15 {{SGDpaper|S000124746}} PMID 18021800</ref><ref name='S000081138'>Huang B, et al. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11(4):424-36 {{SGDpaper|S000081138}} PMID 15769872</ref><ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000069896'>Fichtner L and Schaffrath R (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44(3):865-75
   {{SGDpaper|S000069896}} PMID 11994165</ref>
 <br>

@@ 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=S000007587 YBL071W-A]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000007587 YBL071W-A]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''KTI11 ''

← Older revision		Revision as of 20:02, 21 February 2007
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		+
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		+	<!-- 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>

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 {{PageTop}}
 {|{{Prettytable}} align = 'right' width = '200px'
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr II:89976..90224
 |}
 <br>
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 <br>
+<br>
 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}