Difference between revisions of "YLL026W"

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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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Revision as of 13:02, 21 February 2007

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Systematic name YLL026W
Gene name HSP104
Aliases
Feature type ORF, Verified
Coordinates Chr XII:88622..91348


Description of YLL026W: Heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation[1][2][3][4][5][6]




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References

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  1. Moriyama H, et al. (2000) [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol Cell Biol 20(23):8916-22 SGD PMID 11073991
  2. Parsell DA, et al. (1991) Hsp104 is a highly conserved protein with two essential nucleotide-binding sites. Nature 353(6341):270-3 SGD PMID 1896074
  3. Parsell DA, et al. (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372(6505):475-8 SGD PMID 7984243
  4. Glover JR and Lindquist S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94(1):73-82 SGD PMID 9674429
  5. Chernoff YO, et al. (1995) Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268(5212):880-4 SGD PMID 7754373
  6. Sanchez Y, et al. (1992) Hsp104 is required for tolerance to many forms of stress. EMBO J 11(6):2357-64 SGD PMID 1600951

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