YBR072W
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| Systematic name | YBR072W | |
| Gene name | HSP26 | |
| Aliases | ||
| Feature type | ORF, Verified | |
| Coordinates | Chr II:382027..382671 | |
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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]
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References
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- ↑ 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
- ↑ 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
- ↑ Haslbeck M, et al. (1999) Hsp26: a temperature-regulated chaperone. EMBO J 18(23):6744-51 SGD PMID 10581247
- ↑ 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
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