Difference between revisions of "YNL064C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YNL064C YNL064C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005008 YNL064C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''YDJ1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''YDJ1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
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|nowrap| Chr XIV:507098..505869
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|nowrap| Chr XIV:507097..505868
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005008
 
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'''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
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'''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
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  {{SGDpaper|S000049386}} PMID 7737974</ref>
 
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==Community Commentary==
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=== Interactions ===
 
=== Interactions ===
 
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'''Strain Background''': W303<br>
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'''Strain Background''': W303 (''see [[CommunityW303.html|detailed notes]] from Rodney Rothstein and Stephan Bartsch for the W303 strain used in the study'')
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'''Mutation type(s)''': point mutation (ydj1-151), deletion
 
'''Mutation type(s)''': point mutation (ydj1-151), deletion
  
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==== Genetic ====
 
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YNL064C is suppressed by  FES1 [[Category:Genetic Interaction with FES1]]
 
  
  
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'''Strain Background''': W303<br>
 
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'''Mutation type(s)''': point mutation (ydj1-151), deletion
 
  
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The thermosensitivity and cycloheximide sensitivity of the single deltafes1 and ydj1-151 mutants is partly suppressed in the double mutant. <ref name='S000072758'>Kabani M, et al. (2002) Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol Cell Biol 22(13):4677-89 {{SGDpaper|S000072758}} PMID 12052876</ref> <ref name = 'CAset9225-2003-03-31'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9225 Mehdi Kabani] on 2003-03-31</ref>
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.  
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 14:05, 14 September 2012

Share your knowledge...Edit this entry! <protect>

Systematic name YNL064C
Gene name YDJ1
Aliases HSP40, MAS5
Feature type ORF, Verified
Coordinates Chr XIV:507097..505868
Primary SGDID S000005008


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[1][2][3][4][5][6][7]




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Community Commentary

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Interactions

Genetic

YNL064C is suppressed by FES1


Strain Background: W303 (see detailed notes from Rodney Rothstein and Stephan Bartsch for the W303 strain used in the study)
Mutation type(s): point mutation (ydj1-151), deletion

The thermosensitivity and cycloheximide sensitivity of the single deltafes1 and ydj1-151 mutants is partly suppressed in the double mutant. [8] [9]




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References

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  1. ↑ Caplan AJ and Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21 SGD PMID 1869583
  2. ↑ Caplan AJ, et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55 SGD PMID 1473150
  3. ↑ 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 SGD PMID 22910358
  4. ↑ 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 SGD PMID 11689685
  5. ↑ Kimura Y, et al. (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5 SGD PMID 7761857
  6. ↑ Summers DW, et al. (2009) Prion propagation by Hsp40 molecular chaperones. Prion 3(2):59-64 SGD PMID 19535913
  7. ↑ 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 SGD PMID 7737974
  8. ↑ Kabani M, et al. (2002) Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol Cell Biol 22(13):4677-89 SGD PMID 12052876
  9. ↑ submitted by Mehdi Kabani on 2003-03-31

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