Difference between revisions of "YAL005C"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
 
(Automated import of articles)
Line 23: Line 23:
 
<br>
 
<br>
 
<br>
 
<br>
 +
=== Interactions ===
 +
[[Category:Topic:Interactions]]
 +
==== Physical ====
 +
[[Category:Topic:Interactions:Physical]]
 +
Physical interaction with FES1 [[Category:Physical Interactions with FES1]]<br>
 +
Purified GST-Fes1p interacts with the ADP-bound form of (His6)-Ssa1p in GST pull down assays <ref name='S000072758'>Kabani M, et al. (2002) Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol Cell Biol 22(13):4677-89 {{SGDpaper|S000072758}} PMID 12052876</ref> <ref name = 'CAset9225-2003-03-31'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9225 Mehdi Kabani] on 2003-03-31</ref>
  
 +
{{ShortCenteredHR}}
 +
==== Regulatory ====
 +
[[Category:Topic:Interactions:Regulatory]]
 +
YAL005C is regulated by cns1. [[Category:Regulated by cns1]]Regulatory interaction with cns1 [[Category:Regulatory Interactions with cns1]]<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}}
 +
YAL005C is regulated by Sti1. [[Category:Regulated by Sti1]]Regulatory interaction with Sti1 [[Category:Regulatory Interactions with Sti1]]<br>
 +
Binding of Sti1 to Ssa1 activates the ATPase of Ssa1 by a factor of about 200, which is in contrast to the behaviour of Hop in the mammalian Hsp70 system. Analysis of the underlying activation mechanism revealed that ATP hydrolysis is rate limiting in the Ssa1 ATPase cycle and that this step is accelerated by Sti1. <ref name='S000073412'>Wegele H, et al. (2003) Sti1 is a novel activator of the Ssa proteins. J Biol Chem 278(28):25970-6 {{SGDpaper|S000073412}} PMID 12716905</ref> <ref name = 'CAset9598-2003-09-03'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9598 Dr. Harald Wegele] on 2003-09-03</ref>
 +
 +
{{ShortCenteredHR}}
 +
==== Two Hybrid ====
 +
[[Category:Topic:Interactions:Two Hybrid]]
 +
Two Hybrid interaction with Sti1 [[Category:Two Hybrid Interactions with Sti1]]<br>
 +
With a two hybrid approach and coimmunoprecipitations, we show that Sti1 specifically interacts with the Ssa group of the cytosolic yeast Hsp70 proteins and not with the Ssb, Sse and Ssz group. <ref name='S000073412'>Wegele H, et al. (2003) Sti1 is a novel activator of the Ssa proteins. J Biol Chem 278(28):25970-6 {{SGDpaper|S000073412}} PMID 12716905</ref> <ref name = 'CAset9598-2003-09-03'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9598 Dr. Harald Wegele] on 2003-09-03</ref>
 +
 +
{{ShortCenteredHR}}
 
__TOC__
 
__TOC__
 
==Community Commentary==
 
==Community Commentary==
 
{{CommentaryHelp}}
 
{{CommentaryHelp}}
 +
=== Interactions ===
 +
[[Category:Topic:Interactions]]
 +
==== Physical ====
 +
[[Category:Topic:Interactions:Physical]]
 +
Physical interaction with FES1 [[Category:Physical Interactions with FES1]]<br>
 +
Purified GST-Fes1p interacts with the ADP-bound form of (His6)-Ssa1p in GST pull down assays <ref name='S000072758'>Kabani M, et al. (2002) Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol Cell Biol 22(13):4677-89 {{SGDpaper|S000072758}} PMID 12052876</ref> <ref name = 'CAset9225-2003-03-31'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9225 Mehdi Kabani] on 2003-03-31</ref>
 +
 +
{{ShortCenteredHR}}
 +
==== Regulatory ====
 +
[[Category:Topic:Interactions:Regulatory]]
 +
YAL005C is regulated by cns1. [[Category:Regulated by cns1]]Regulatory interaction with cns1 [[Category:Regulatory Interactions with cns1]]<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}}
 +
YAL005C is regulated by Sti1. [[Category:Regulated by Sti1]]Regulatory interaction with Sti1 [[Category:Regulatory Interactions with Sti1]]<br>
 +
Binding of Sti1 to Ssa1 activates the ATPase of Ssa1 by a factor of about 200, which is in contrast to the behaviour of Hop in the mammalian Hsp70 system. Analysis of the underlying activation mechanism revealed that ATP hydrolysis is rate limiting in the Ssa1 ATPase cycle and that this step is accelerated by Sti1. <ref name='S000073412'>Wegele H, et al. (2003) Sti1 is a novel activator of the Ssa proteins. J Biol Chem 278(28):25970-6 {{SGDpaper|S000073412}} PMID 12716905</ref> <ref name = 'CAset9598-2003-09-03'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9598 Dr. Harald Wegele] on 2003-09-03</ref>
 +
 +
{{ShortCenteredHR}}
 +
==== Two Hybrid ====
 +
[[Category:Topic:Interactions:Two Hybrid]]
 +
Two Hybrid interaction with Sti1 [[Category:Two Hybrid Interactions with Sti1]]<br>
 +
With a two hybrid approach and coimmunoprecipitations, we show that Sti1 specifically interacts with the Ssa group of the cytosolic yeast Hsp70 proteins and not with the Ssb, Sse and Ssz group. <ref name='S000073412'>Wegele H, et al. (2003) Sti1 is a novel activator of the Ssa proteins. J Biol Chem 278(28):25970-6 {{SGDpaper|S000073412}} PMID 12716905</ref> <ref name = 'CAset9598-2003-09-03'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9598 Dr. Harald Wegele] on 2003-09-03</ref>
  
 +
{{ShortCenteredHR}}
 
==References==
 
==References==
 
<!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 
<!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 
{{RefHelp}}
 
{{RefHelp}}

Revision as of 16:05, 23 January 2007

Share your knowledge...Edit this entry!

Systematic name YAL005C
Gene name SSA1
Aliases YG100
Feature type ORF, Verified
Coordinates Chr I:141433..139505
Don't edit this box! It's automatically regenerated, and edits will be lost when the update script runs.


Description of YAL005C: ATPase involved in protein folding and nuclear localization signal (NLS)-directed nuclear transport; member of heat shock protein 70 (HSP70) family; forms a chaperone complex with Ydj1p; localized to the nucleus, cytoplasm, and cell wall[1][2][3][4][5]



Interactions

Physical

Physical interaction with FES1
Purified GST-Fes1p interacts with the ADP-bound form of (His6)-Ssa1p in GST pull down assays [6] [7]


Regulatory

YAL005C is regulated by cns1.Regulatory interaction with cns1
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. [8] [9]


YAL005C is regulated by Sti1.Regulatory interaction with Sti1
Binding of Sti1 to Ssa1 activates the ATPase of Ssa1 by a factor of about 200, which is in contrast to the behaviour of Hop in the mammalian Hsp70 system. Analysis of the underlying activation mechanism revealed that ATP hydrolysis is rate limiting in the Ssa1 ATPase cycle and that this step is accelerated by Sti1. [10] [11]


Two Hybrid

Two Hybrid interaction with Sti1
With a two hybrid approach and coimmunoprecipitations, we show that Sti1 specifically interacts with the Ssa group of the cytosolic yeast Hsp70 proteins and not with the Ssb, Sse and Ssz group. [10] [11]


Community Commentary

About Community Commentary. Please share your knowledge!

Interactions

Physical

Physical interaction with FES1
Purified GST-Fes1p interacts with the ADP-bound form of (His6)-Ssa1p in GST pull down assays [6] [7]


Regulatory

YAL005C is regulated by cns1.Regulatory interaction with cns1
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. [8] [9]


YAL005C is regulated by Sti1.Regulatory interaction with Sti1
Binding of Sti1 to Ssa1 activates the ATPase of Ssa1 by a factor of about 200, which is in contrast to the behaviour of Hop in the mammalian Hsp70 system. Analysis of the underlying activation mechanism revealed that ATP hydrolysis is rate limiting in the Ssa1 ATPase cycle and that this step is accelerated by Sti1. [10] [11]


Two Hybrid

Two Hybrid interaction with Sti1
With a two hybrid approach and coimmunoprecipitations, we show that Sti1 specifically interacts with the Ssa group of the cytosolic yeast Hsp70 proteins and not with the Ssb, Sse and Ssz group. [10] [11]


References

See Help:References on how to add references

  1. Bush GL and Meyer DI (1996) The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. J Cell Biol 135(5):1229-37 SGD PMID 8947547
  2. 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
  3. Shulga N, et al. (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7 SGD PMID 10347213
  4. Kim S, et al. (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci U S A 95(22):12860-5 SGD PMID 9789005
  5. Lopez-Ribot JL and Chaffin WL (1996) Members of the Hsp70 family of proteins in the cell wall of Saccharomyces cerevisiae. J Bacteriol 178(15):4724-6 SGD PMID 8755907
  6. 6.0 6.1 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
  7. 7.0 7.1 submitted by Mehdi Kabani on 2003-03-31
  8. 8.0 8.1 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. 9.0 9.1 submitted by Dr. Harald Wegele on 2004-07-15
  10. 10.0 10.1 10.2 10.3 Wegele H, et al. (2003) Sti1 is a novel activator of the Ssa proteins. J Biol Chem 278(28):25970-6 SGD PMID 12716905
  11. 11.0 11.1 11.2 11.3 submitted by Dr. Harald Wegele on 2003-09-03

See Help:Categories on how to add the wiki page for this gene to a Category