Difference between revisions of "YLL026W"
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| − | '''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<ref name='S000047554'>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 {{SGDpaper|S000047554}} PMID 7754373</ref><ref name='S000048256'>Glover JR and Lindquist S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94(1):73-82 {{SGDpaper|S000048256}} PMID 9674429</ref><ref name='S000059594'>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 {{SGDpaper|S000059594}} PMID 11073991</ref><ref name='S000053352'>Parsell DA, et al. (1991) Hsp104 is a highly conserved protein with two essential nucleotide-binding sites. Nature 353(6341):270-3 {{SGDpaper|S000053352}} PMID 1896074</ref><ref name='S000050547'>Parsell DA, et al. (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372(6505):475-8 {{SGDpaper|S000050547}} PMID 7984243</ref><ref name='S000042075'>Sanchez Y, et al. (1992) Hsp104 is required for tolerance to many forms of stress. EMBO J 11(6):2357-64 | + | '''Description of YLL026W:''' Disaggregase; 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<ref name='S000047554'>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 {{SGDpaper|S000047554}} PMID 7754373</ref><ref name='S000048256'>Glover JR and Lindquist S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94(1):73-82 {{SGDpaper|S000048256}} PMID 9674429</ref><ref name='S000059594'>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 {{SGDpaper|S000059594}} PMID 11073991</ref><ref name='S000053352'>Parsell DA, et al. (1991) Hsp104 is a highly conserved protein with two essential nucleotide-binding sites. Nature 353(6341):270-3 {{SGDpaper|S000053352}} PMID 1896074</ref><ref name='S000050547'>Parsell DA, et al. (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372(6505):475-8 {{SGDpaper|S000050547}} PMID 7984243</ref><ref name='S000042075'>Sanchez Y, et al. (1992) Hsp104 is required for tolerance to many forms of stress. EMBO J 11(6):2357-64 |
{{SGDpaper|S000042075}} PMID 1600951</ref> | {{SGDpaper|S000042075}} PMID 1600951</ref> | ||
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Latest revision as of 13:05, 1 August 2012
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| Systematic name | YLL026W |
| Gene name | HSP104 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:88623..91349 |
| Primary SGDID | S000003949 |
Description of YLL026W: Disaggregase; 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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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Parsell DA, et al. (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372(6505):475-8 SGD PMID 7984243
- ↑ 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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