Difference between revisions of "YBR072W"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
(Automated import of articles)
 
(6 intermediate revisions by the same user not shown)
Line 4: Line 4:
 
{|{{Prettytable}} align = 'right' width = '200px'
 
{|{{Prettytable}} align = 'right' width = '200px'
 
|-
 
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000276 YBR072W]  
+
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000276 YBR072W]  
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HSP26 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HSP26 ''
Line 13: Line 13:
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr II:382027..382671
+
|nowrap| Chr II:382030..382674
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000276
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000276
 
|}
 
|}
 
<br>
 
<br>
'''Description of YBR072W:''' Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires a heat-induced conformational change; not expressed in unstressed cells<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 {{SGDpaper|S000117332}} PMID 16843901</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='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
+
'''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
  {{SGDpaper|S000040265}} PMID 1561840</ref>
+
  {{SGDpaper|S000117332}} PMID 16843901</ref>
 
<br>
 
<br>
 
<br>
 
<br>

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]




</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. 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

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