Difference between revisions of "YBR072W"
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| − | '''Description of YBR072W:''' Small heat shock protein with chaperone activity that | + | '''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 |
{{SGDpaper|S000040265}} PMID 1561840</ref> | {{SGDpaper|S000040265}} PMID 1561840</ref> | ||
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Revision as of 13:05, 26 July 2007
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| Systematic name | YBR072W |
| Gene name | HSP26 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr II:382027..382671 |
| 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 a heat-induced conformational change; not expressed in unstressed cells[1][2][3][4]
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Contents
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. [5] [6]
Other Topic: expression
Specifically lower expression in nitrogen limited chemostat cultures versus nitrogen excess. [5] [6]
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References
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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 5.0 5.1 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
- ↑ 6.0 6.1 submitted by Viktor Boer on 2003-07-25
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