Difference between revisions of "YNL064C"
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− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.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''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XIV:507098..505869 | |nowrap| Chr XIV:507098..505869 | ||
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+ | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005008 | ||
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<br> | <br> | ||
− | '''Description of | + | '''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> | {{SGDpaper|S000048634}} PMID 7761857</ref> | ||
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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<protect> | <protect> |
Revision as of 07:46, 27 February 2007
Share your knowledge...Edit this entry! <protect>
Systematic name | YNL064C |
Gene name | YDJ1 |
Aliases | HSP40, MAS5 |
Feature type | ORF, Verified |
Coordinates | Chr XIV:507098..505869 |
Primary SGDID | S000005008 |
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[1][2][3][4][5]
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Community Commentary
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Interactions
Genetic
YNL064C is suppressed by FES1
Strain Background: W303
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. [6] [7]
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References
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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ submitted by Mehdi Kabani on 2003-03-31
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