Difference between revisions of "YBR155W"
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| + | === Interactions === | ||
| + | [[Category:Topic:Interactions]] | ||
| + | ==== Genetic ==== | ||
| + | [[Category:Topic:Interactions:Genetic]] | ||
| + | YBR155W is a suppressor of CPR7 [[Category:Genetic Interaction with CPR7]] | ||
| + | <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 = 'CAset1441-2003-02-04'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=1441 Kara Dolinski] on 2003-02-04</ref> | ||
| + | |||
| + | {{ShortCenteredHR}} | ||
| + | ==== Physical ==== | ||
| + | [[Category:Topic:Interactions:Physical]] | ||
| + | Physical interaction with Hsp82 [[Category:Physical Interactions with Hsp82]]<br> | ||
| + | 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> | ||
| + | |||
| + | {{ShortCenteredHR}} | ||
| + | ==== Regulatory ==== | ||
| + | [[Category:Topic:Interactions:Regulatory]] | ||
| + | Regulatory interaction with ssa1 [[Category:Regulatory Interactions with ssa1]]<br> | ||
| + | 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. <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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| + | {{ShortCenteredHR}} | ||
__TOC__ | __TOC__ | ||
==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
| + | === Interactions === | ||
| + | [[Category:Topic:Interactions]] | ||
| + | ==== Genetic ==== | ||
| + | [[Category:Topic:Interactions:Genetic]] | ||
| + | YBR155W is a suppressor of CPR7 [[Category:Genetic Interaction with CPR7]] | ||
| + | |||
| + | <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 = 'CAset1441-2003-02-04'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=1441 Kara Dolinski] on 2003-02-04</ref> | ||
| + | |||
| + | {{ShortCenteredHR}} | ||
| + | ==== Physical ==== | ||
| + | [[Category:Topic:Interactions:Physical]] | ||
| + | Physical interaction with Hsp82 [[Category:Physical Interactions with Hsp82]]<br> | ||
| + | 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> | ||
| + | |||
| + | {{ShortCenteredHR}} | ||
| + | ==== Regulatory ==== | ||
| + | [[Category:Topic:Interactions:Regulatory]] | ||
| + | Regulatory interaction with ssa1 [[Category:Regulatory Interactions with ssa1]]<br> | ||
| + | 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. <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> | ||
| + | {{ShortCenteredHR}} | ||
==References== | ==References== | ||
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Revision as of 16:05, 23 January 2007
Share your knowledge...Edit this entry!
| Systematic name | YBR155W | |
| Gene name | CNS1 | |
| Aliases | ||
| Feature type | ORF, Verified | |
| Coordinates | Chr II:549765..550922 | |
| Don't edit this box! It's automatically regenerated, and edits will be lost when the update script runs. | ||
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]
Interactions
Genetic
YBR155W is a suppressor of CPR7
[3] [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. [1] [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. [1] [6]
Contents
Community Commentary
About Community Commentary. Please share your knowledge!
Interactions
Genetic
YBR155W is a suppressor of CPR7
[3] [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. [1] [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. [1] [6]
References
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- ↑ 1.0 1.1 1.2 1.3 1.4 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
- ↑ 3.0 3.1 3.2 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
- ↑ 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
- ↑ 5.0 5.1 submitted by Kara Dolinski on 2003-02-04
- ↑ 6.0 6.1 6.2 6.3 submitted by Dr. Harald Wegele on 2004-07-15
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