YNL064C - Revision history

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@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNL064C:''' Type I HSP40 co-chaperone involved in regulation of the HSP90 and HSP70 functions; involved in protein translocation across membranes; member of the DnaJ family<ref name='S000051244'>Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 {{SGDpaper|S000051244}} PMID 1869583</ref><ref name='S000056529'>Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 {{SGDpaper|S000056529}} PMID 1473150</ref><ref name='S000068862'>Hon T, et al. (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32 {{SGDpaper|S000068862}} PMID 11689685</ref><ref name='S000048634'>Kimura Y, et al. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5 {{SGDpaper|S000048634}} PMID 7761857</ref><ref name='S000130690'>Summers DW, et al. (2009) Prion propagation by Hsp40 molecular chaperones. Prion 3(2):59-64 {{SGDpaper|S000130690}} PMID 19535913</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
+'''Description of YNL064C:''' Type I HSP40 co-chaperone; involved in regulation of HSP90 and HSP70 functions; critical for determining cell size at Start as a function of growth rate; involved in protein translocation across membranes; member of the DnaJ family<ref name='S000051244'>Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 {{SGDpaper|S000051244}} PMID 1869583</ref><ref name='S000056529'>Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 {{SGDpaper|S000056529}} PMID 1473150</ref><ref name='S000150594'>Ferrezuelo F, et al. (2012) The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation. Nat Commun 3():1012 {{SGDpaper|S000150594}} PMID 22910358</ref><ref name='S000068862'>Hon T, et al. (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32 {{SGDpaper|S000068862}} PMID 11689685</ref><ref name='S000048634'>Kimura Y, et al. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5 {{SGDpaper|S000048634}} PMID 7761857</ref><ref name='S000130690'>Summers DW, et al. (2009) Prion propagation by Hsp40 molecular chaperones. Prion 3(2):59-64 {{SGDpaper|S000130690}} PMID 19535913</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
   {{SGDpaper|S000049386}} PMID 7737974</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=S000005008 YNL064C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005008 YNL064C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''YDJ1 ''

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNL064C:''' Protein chaperone involved in regulation of the HSP90 and HSP70 functions; involved in protein translocation across membranes; member of the DnaJ family<ref name='S000051244'>Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 {{SGDpaper|S000051244}} PMID 1869583</ref><ref name='S000056529'>Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 {{SGDpaper|S000056529}} PMID 1473150</ref><ref name='S000068862'>Hon T, et al. (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32 {{SGDpaper|S000068862}} PMID 11689685</ref><ref name='S000048634'>Kimura Y, et al. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5 {{SGDpaper|S000048634}} PMID 7761857</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
+'''Description of YNL064C:''' Type I HSP40 co-chaperone involved in regulation of the HSP90 and HSP70 functions; involved in protein translocation across membranes; member of the DnaJ family<ref name='S000051244'>Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 {{SGDpaper|S000051244}} PMID 1869583</ref><ref name='S000056529'>Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 {{SGDpaper|S000056529}} PMID 1473150</ref><ref name='S000068862'>Hon T, et al. (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32 {{SGDpaper|S000068862}} PMID 11689685</ref><ref name='S000048634'>Kimura Y, et al. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5 {{SGDpaper|S000048634}} PMID 7761857</ref><ref name='S000130690'>Summers DW, et al. (2009) Prion propagation by Hsp40 molecular chaperones. Prion 3(2):59-64 {{SGDpaper|S000130690}} PMID 19535913</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
   {{SGDpaper|S000049386}} PMID 7737974</ref>
 <br>

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIV:507099..505870
+|nowrap| Chr XIV:507097..505868
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005008

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNL064C:''' Protein chaperone involved in regulation of the HSP90 and HSP70 functions; involved in protein translocation across membranes; member of the DnaJ family<ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9 {{SGDpaper|S000049386}} PMID 7737974</ref><ref name='S000048634'>Kimura Y, et al. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5 {{SGDpaper|S000048634}} PMID 7761857</ref><ref name='S000051244'>Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 {{SGDpaper|S000051244}} PMID 1869583</ref><ref name='S000056529'>Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 {{SGDpaper|S000056529}} PMID 1473150</ref><ref name='S000068862'>Hon T, et al. (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32
+'''Description of YNL064C:''' Protein chaperone involved in regulation of the HSP90 and HSP70 functions; involved in protein translocation across membranes; member of the DnaJ family<ref name='S000051244'>Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 {{SGDpaper|S000051244}} PMID 1869583</ref><ref name='S000056529'>Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 {{SGDpaper|S000056529}} PMID 1473150</ref><ref name='S000068862'>Hon T, et al. (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32 {{SGDpaper|S000068862}} PMID 11689685</ref><ref name='S000048634'>Kimura Y, et al. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5 {{SGDpaper|S000048634}} PMID 7761857</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
-  {{SGDpaper|S000068862}} PMID 11689685</ref>
+  {{SGDpaper|S000049386}} PMID 7737974</ref>
 <br>
 <br>

← Older revision		Revision as of 14:29, 19 June 2009
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−	'''Strain Background''': W303<br>	+	'''Strain Background''': W303 (''see [[CommunityW303.html\|detailed notes]] from Rodney Rothstein and Stephan Bartsch for the W303 strain used in the study'')
		+	<br>
	'''Mutation type(s)''': point mutation (ydj1-151), deletion		'''Mutation type(s)''': point mutation (ydj1-151), deletion

@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YNL064C YNL064C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005008 YNL064C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''YDJ1 ''
@@ Line 14: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XIV:507098..505869
 |}
 <br>
-'''Description of {{PAGENAME}}:''' Protein chaperone involved in regulation of the HSP90 and HSP70 functions; involved in protein translocation across membranes; member of the DnaJ family<ref name='S000068862'>Hon T, et al. (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32 {{SGDpaper|S000068862}} PMID 11689685</ref><ref name='S000056529'>Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 {{SGDpaper|S000056529}} PMID 1473150</ref><ref name='S000051244'>Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 {{SGDpaper|S000051244}} PMID 1869583</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9 {{SGDpaper|S000049386}} PMID 7737974</ref><ref name='S000048634'>Kimura Y, et al. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5
+'''Description of YNL064C:''' Protein chaperone involved in regulation of the HSP90 and HSP70 functions; involved in protein translocation across membranes; member of the DnaJ family<ref name='S000068862'>Hon T, et al. (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32 {{SGDpaper|S000068862}} PMID 11689685</ref><ref name='S000056529'>Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 {{SGDpaper|S000056529}} PMID 1473150</ref><ref name='S000051244'>Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 {{SGDpaper|S000051244}} PMID 1869583</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9 {{SGDpaper|S000049386}} PMID 7737974</ref><ref name='S000048634'>Kimura Y, et al. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5
   {{SGDpaper|S000048634}} PMID 7761857</ref>
 <br>
@@ Line 49: / Line 51: @@
 J Biol Chem 278(5):3265-74</ref>
 -->
 <protect>

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