Difference between revisions of "YBR155W"
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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=S000000359 YBR155W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CNS1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CNS1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr II: | + | |nowrap| Chr II:549771..550928 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000359 | ||
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| − | '''Description of | + | '''Description of YBR155W:''' TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70) and stimulates the ATPase activity of SSA1, ts mutants reduce Hsp82p function while over expression suppresses the phenotypes of an HSP82 ts allele and a cpr7 deletion<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='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='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='S000044986'>Nathan DF, et al. (1999) Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proc Natl Acad Sci U S A 96(4):1409-14 |
{{SGDpaper|S000044986}} PMID 9990037</ref> | {{SGDpaper|S000044986}} PMID 9990037</ref> | ||
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| + | <!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation --> | ||
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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. | ||
| + | J Biol Chem 278(5):3265-74</ref> | ||
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Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YBR155W |
| Gene name | CNS1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr II:549771..550928 |
| Primary SGDID | S000000359 |
Description of YBR155W: TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70) and stimulates the ATPase activity of SSA1, ts mutants reduce Hsp82p function while over expression suppresses the phenotypes of an HSP82 ts allele and a cpr7 deletion[1][2][3][4]
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Contents
Community Commentary
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Interactions
Genetic
YBR155W is a suppressor of CPR7
[1] [5]
Physical
Physical interaction with Hsp82
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. [2] [6]
Regulatory
Regulatory interaction with ssa1
Cns1 exhibits no influence on the ATPase of Hsp90. However, it activates the ATPase of Ssa1 up to 30-fold by accelerating the rate-limiting ATP hydrolysis step. This stimulating effect is mediated by the N-terminal TPR-containing part of Cns1, whereas the C-terminal part showed no effect. [2] [6]
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References
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- ↑ 1.0 1.1 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
- ↑ 2.0 2.1 2.2 Hainzl O, et al. (2004) Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem 279(22):23267-73 SGD PMID 15044454
- ↑ 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
- ↑ Nathan DF, et al. (1999) Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proc Natl Acad Sci U S A 96(4):1409-14 SGD PMID 9990037
- ↑ submitted by Kara Dolinski on 2003-02-04
- ↑ 6.0 6.1 submitted by Dr. Harald Wegele on 2004-07-15
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