Difference between revisions of "YBR072W"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
(Automated import of articles)
Line 1: Line 1:
 
<!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN-->
 
<!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN-->
 
{{PageTop}}
 
{{PageTop}}
 +
<protect>
 
{|{{Prettytable}} align = 'right' width = '200px'
 
{|{{Prettytable}} align = 'right' width = '200px'
 
|-
 
|-
Line 13: Line 14:
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|nowrap| Chr II:382027..382671
 
|nowrap| Chr II:382027..382671
|-
 
|colspan = '3'|{{Don'tEditThisBox}}
 
 
|}
 
|}
 
<br>
 
<br>
Line 23: Line 22:
 
<br>
 
<br>
 
<br>
 
<br>
 +
<br>
 +
</protect>
 
__TOC__
 
__TOC__
 
==Community Commentary==
 
==Community Commentary==
Line 40: Line 41:
  
 
{{ShortCenteredHR}}
 
{{ShortCenteredHR}}
 +
 +
<protect>
 
==References==
 
==References==
 
<!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 
<!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 
{{RefHelp}}
 
{{RefHelp}}
 +
</protect>

Revision as of 07:17, 30 January 2007

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

Systematic name YBR072W
Gene name HSP26
Aliases
Feature type ORF, Verified
Coordinates Chr II:382027..382671


Description of YBR072W: 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[1][2][3][4][5]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!

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]


<protect>

References

See Help:References on how to add references

  1. 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 SGD PMID 14722093
  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. Haslbeck M, et al. (1999) Hsp26: a temperature-regulated chaperone. EMBO J 18(23):6744-51 SGD PMID 10581247
  5. 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
  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

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