Difference between revisions of "YNL064C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |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''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XIV: | + | |nowrap| Chr XIV:507097..505868 |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005008 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005008 | ||
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| − | '''Description of YNL064C:''' | + | '''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| | + | {{SGDpaper|S000049386}} PMID 7737974</ref> |
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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 | ||
Latest revision as of 13:05, 14 September 2012
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| 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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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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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Summers DW, et al. (2009) Prion propagation by Hsp40 molecular chaperones. Prion 3(2):59-64 SGD PMID 19535913
- ↑ 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
- ↑ 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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