Difference between revisions of "YLL026W"
SGDwikiBot (talk | contribs) (Automated import of articles) |
SGDwikiBot (talk | contribs) (Automated import of articles) |
||
(7 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
<!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | ||
{{PageTop}} | {{PageTop}} | ||
+ | <protect> | ||
{|{{Prettytable}} align = 'right' width = '200px' | {|{{Prettytable}} align = 'right' width = '200px' | ||
|- | |- | ||
− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003949 YLL026W] |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP104 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP104 '' | ||
Line 12: | Line 13: | ||
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
− | |nowrap| Chr XII: | + | |nowrap| Chr XII:88623..91349 |
|- | |- | ||
− | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003949 |
|} | |} | ||
<br> | <br> | ||
− | '''Description of | + | '''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> | ||
<br> | <br> | ||
Line 23: | Line 24: | ||
<br> | <br> | ||
<br> | <br> | ||
− | + | <br> | |
+ | </protect> | ||
__TOC__ | __TOC__ | ||
==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
+ | |||
+ | |||
+ | |||
+ | <!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation --> | ||
+ | <!-- | ||
+ | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
+ | <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. | ||
+ | J Biol Chem 278(5):3265-74</ref> | ||
+ | --> | ||
+ | |||
+ | |||
+ | |||
+ | <protect> | ||
==References== | ==References== | ||
<!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | <!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | ||
{{RefHelp}} | {{RefHelp}} | ||
+ | </protect> |
Latest revision as of 14:05, 1 August 2012
Share your knowledge...Edit this entry! <protect>
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]
</protect>
Contents
Community Commentary
About Community Commentary. Please share your knowledge!
<protect>
References
See Help:References on how to add references
- ↑ 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
See Help:Categories on how to add the wiki page for this gene to a Category </protect>