Difference between revisions of "YPL240C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YPL240C YPL240C]  
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|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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'''Description of {{PAGENAME}}:''' Cytoplasmic chaperone (Hsp90 family) required for pheromone signaling and negative regulation of Hsf1p; docks with the mitochondrial import receptor Tom70p for preprotein delivery; interacts with co-chaperones Cns1p, Cpr6p, Cpr7p, and Sti1p<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|S000072572}} PMID 12526792</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='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='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='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='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
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'''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|S000047779}} PMID 9819421</ref>
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  {{SGDpaper|S000072572}} PMID 12526792</ref>
 
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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.
 
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Latest revision as of 06:45, 23 January 2012

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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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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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  1. 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
  2. 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
  3. Louvion JF, et al. (1998) Hsp90 is required for pheromone signaling in yeast. Mol Biol Cell 9(11):3071-83 SGD PMID 9802897
  4. 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
  5. 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
  6. Toogun OA, et al. (2008) The hsp90 molecular chaperone modulates multiple telomerase activities. Mol Cell Biol 28(1):457-67 SGD PMID 17954556
  7. 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
  8. Hainzl O, et al. (2004) Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem 279(22):23267-73 SGD PMID 15044454
  9. submitted by Dr. Harald Wegele on 2004-07-15

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References

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