Difference between revisions of "YBR072W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YBR072W YBR072W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000276 YBR072W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HSP26 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HSP26 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr II:382027..382671
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|nowrap| Chr II:382030..382674
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000276
 
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'''Description of {{PAGENAME}}:''' Small heat shock protein with chaperone activity that is regulated by a heat induced transition from an inactive oligomeric (24-mer) complex to an active dimer; induced by heat, upon entry into stationary phase, and during sporulation<ref name='S000075678'>Stromer T, et al. (2004) Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J Biol Chem 279(12):11222-8 {{SGDpaper|S000075678}} PMID 14722093</ref><ref name='S000050750'>Rossi JM and Lindquist S (1989) The intracellular location of yeast heat-shock protein 26 varies with metabolism. J Cell Biol 108(2):425-39 {{SGDpaper|S000050750}} PMID 2645298</ref><ref name='S000047920'>Susek RE and Lindquist S (1990) Transcriptional derepression of the Saccharomyces cerevisiae HSP26 gene during heat shock. Mol Cell Biol 10(12):6362-73 {{SGDpaper|S000047920}} PMID 2123293</ref><ref name='S000043785'>Haslbeck M, et al. (1999) Hsp26: a temperature-regulated chaperone. EMBO J 18(23):6744-51 {{SGDpaper|S000043785}} PMID 10581247</ref><ref name='S000040265'>Bentley NJ, et al. (1992) The small heat-shock protein Hsp26 of Saccharomyces cerevisiae assembles into a high molecular weight aggregate. Yeast 8(2):95-106
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'''Description of YBR072W:''' Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires heat-induced conformational change; also has mRNA binding activity<ref name='S000040265'>Bentley NJ, et al. (1992) The small heat-shock protein Hsp26 of Saccharomyces cerevisiae assembles into a high molecular weight aggregate. Yeast 8(2):95-106 {{SGDpaper|S000040265}} PMID 1561840</ref><ref name='S000050750'>Rossi JM and Lindquist S (1989) The intracellular location of yeast heat-shock protein 26 varies with metabolism. J Cell Biol 108(2):425-39 {{SGDpaper|S000050750}} PMID 2645298</ref><ref name='S000047920'>Susek RE and Lindquist S (1990) Transcriptional derepression of the Saccharomyces cerevisiae HSP26 gene during heat shock. Mol Cell Biol 10(12):6362-73 {{SGDpaper|S000047920}} PMID 2123293</ref><ref name='S000136456'>Tsvetanova NG, et al. (2010) Proteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae.LID - e12671 [pii] PLoS One 5(9) {{SGDpaper|S000136456}} PMID 20844764</ref><ref name='S000117332'>White HE, et al. (2006) Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Structure 14(7):1197-204
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  {{SGDpaper|S000117332}} PMID 16843901</ref>
 
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==Community Commentary==
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=== DNA and RNA Details ===
 
=== DNA and RNA Details ===
 
[[Category:Topic:DNA and RNA Details]]
 
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==Community Commentary==
 
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=== DNA and RNA Details ===
 
[[Category:Topic:DNA and RNA Details]]
 
==== Other DNA and RNA Details ====
 
[[Category:Topic:DNA and RNA Details:Other DNA and RNA Details]]
 
'''Other Topic''': expression [[Category:Topic:expression]]
 
  
Specifically higher expression in carbon limited chemostat cultures versus carbon excess. <ref name='S000073646'>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 {{SGDpaper|S000073646}} PMID 12414795</ref> <ref name = 'CAset9153-2003-07-25'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9153 Viktor Boer] on 2003-07-25</ref>
 
  
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'''Other Topic''': expression [[Category:Topic:expression]]
 
  
Specifically lower expression in nitrogen limited chemostat cultures versus nitrogen excess. <ref name='S000073646'>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 {{SGDpaper|S000073646}} PMID 12414795</ref> <ref name = 'CAset9153-2003-07-25'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9153 Viktor Boer] on 2003-07-25</ref>
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 07:45, 23 January 2012

Share your knowledge...Edit this entry! <protect>

Systematic name YBR072W
Gene name HSP26
Aliases
Feature type ORF, Verified
Coordinates Chr II:382030..382674
Primary SGDID S000000276


Description of YBR072W: Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires heat-induced conformational change; also has mRNA binding activity[1][2][3][4][5]




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Community Commentary

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DNA and RNA Details

Other DNA and RNA Details

Other Topic: expression

Specifically higher expression in carbon limited chemostat cultures versus carbon excess. [6] [7]


Other Topic: expression

Specifically lower expression in nitrogen limited chemostat cultures versus nitrogen excess. [6] [7]





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References

See Help:References on how to add references

  1. Bentley NJ, et al. (1992) The small heat-shock protein Hsp26 of Saccharomyces cerevisiae assembles into a high molecular weight aggregate. Yeast 8(2):95-106 SGD PMID 1561840
  2. Rossi JM and Lindquist S (1989) The intracellular location of yeast heat-shock protein 26 varies with metabolism. J Cell Biol 108(2):425-39 SGD PMID 2645298
  3. Susek RE and Lindquist S (1990) Transcriptional derepression of the Saccharomyces cerevisiae HSP26 gene during heat shock. Mol Cell Biol 10(12):6362-73 SGD PMID 2123293
  4. Tsvetanova NG, et al. (2010) Proteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae.LID - e12671 [pii] PLoS One 5(9) SGD PMID 20844764
  5. White HE, et al. (2006) Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Structure 14(7):1197-204 SGD PMID 16843901
  6. 6.0 6.1 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 SGD PMID 12414795
  7. 7.0 7.1 submitted by Viktor Boer on 2003-07-25

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