Difference between revisions of "YPL240C"
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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=S000006161 YPL240C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP82 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP82 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XVI:98625..96496 | |nowrap| Chr XVI:98625..96496 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000006161 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YPL240C:''' Hsp90 chaperone required for pheromone signaling and negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding and nucleotide addition; interacts with Cns1p, Cpr6p, Cpr7p, Sti1p<ref name='S000047779'>Dolinski KJ, et al. (1998) CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90. Mol Cell Biol 18(12):7344-52 {{SGDpaper|S000047779}} PMID 9819421</ref><ref name='S000049475'>Duina AA, et al. (1998) Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. J Biol Chem 273(30):18974-8 {{SGDpaper|S000049475}} PMID 9668076</ref><ref name='S000052578'>Louvion JF, et al. (1998) Hsp90 is required for pheromone signaling in yeast. Mol Biol Cell 9(11):3071-83 {{SGDpaper|S000052578}} PMID 9802897</ref><ref name='S000047783'>Marsh JA, et al. (1998) Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells. Mol Cell Biol 18(12):7353-9 {{SGDpaper|S000047783}} PMID 9819422</ref><ref name='S000053355'>Prodromou C, et al. (1999) Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J 18(3):754-62 {{SGDpaper|S000053355}} PMID 9927435</ref><ref name='S000124509'>Toogun OA, et al. (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol Cell Biol 28(1):457-67 {{SGDpaper|S000124509}} PMID 17954556</ref><ref name='S000072572'>Young JC, et al. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112(1):41-50 |
| − | {{SGDpaper| | + | {{SGDpaper|S000072572}} PMID 12526792</ref> |
<br> | <br> | ||
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[[Category:Topic:Interactions:Physical]] | [[Category:Topic:Interactions:Physical]] | ||
Physical interaction with cns1 [[Category:Physical Interactions with cns1]]<br> | Physical interaction with cns1 [[Category:Physical Interactions with cns1]]<br> | ||
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Cns1 binds both to Hsp90 and to the yeast Hsp70 protein Ssa1 with comparable affinities. This is reminiscent of Sti1, another TPR-containing co-chaperone. <ref name='S000076436'>Hainzl O, et al. (2004) Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem 279(22):23267-73 {{SGDpaper|S000076436}} PMID 15044454</ref> <ref name = 'CAset9598-2004-07-15'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9598 Dr. Harald Wegele] on 2004-07-15</ref> | Cns1 binds both to Hsp90 and to the yeast Hsp70 protein Ssa1 with comparable affinities. This is reminiscent of Sti1, another TPR-containing co-chaperone. <ref name='S000076436'>Hainzl O, et al. (2004) Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem 279(22):23267-73 {{SGDpaper|S000076436}} PMID 15044454</ref> <ref name = 'CAset9598-2004-07-15'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9598 Dr. Harald Wegele] on 2004-07-15</ref> | ||
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| − | + | ==References== | |
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Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YPL240C |
| Gene name | HSP82 |
| Aliases | HSP90 |
| Feature type | ORF, Verified |
| Coordinates | Chr XVI:98625..96496 |
| Primary SGDID | S000006161 |
Description of YPL240C: Hsp90 chaperone required for pheromone signaling and negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding and nucleotide addition; interacts with Cns1p, Cpr6p, Cpr7p, Sti1p[1][2][3][4][5][6][7]
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Community Commentary
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Interactions
Physical
Physical interaction with cns1
Cns1 binds both to Hsp90 and to the yeast Hsp70 protein Ssa1 with comparable affinities. This is reminiscent of Sti1, another TPR-containing co-chaperone. [8] [9]
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References
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- ↑ Dolinski KJ, et al. (1998) CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90. Mol Cell Biol 18(12):7344-52 SGD PMID 9819421
- ↑ Duina AA, et al. (1998) Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. J Biol Chem 273(30):18974-8 SGD PMID 9668076
- ↑ Louvion JF, et al. (1998) Hsp90 is required for pheromone signaling in yeast. Mol Biol Cell 9(11):3071-83 SGD PMID 9802897
- ↑ Marsh JA, et al. (1998) Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells. Mol Cell Biol 18(12):7353-9 SGD PMID 9819422
- ↑ Prodromou C, et al. (1999) Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J 18(3):754-62 SGD PMID 9927435
- ↑ Toogun OA, et al. (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol Cell Biol 28(1):457-67 SGD PMID 17954556
- ↑ Young JC, et al. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112(1):41-50 SGD PMID 12526792
- ↑ Hainzl O, et al. (2004) Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem 279(22):23267-73 SGD PMID 15044454
- ↑ submitted by Dr. Harald Wegele on 2004-07-15
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<protect>
References
See Help:References on how to add references
See Help:Categories on how to add the wiki page for this gene to a Category </protect>
