Difference between revisions of "YNL209W"
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− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005153 YNL209W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SSB2 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SSB2 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
− | |nowrap| Chr XIV: | + | |nowrap| Chr XIV:252059..253900 |
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− | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005153 |
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− | '''Description of | + | '''Description of YNL209W:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in the folding of newly-synthesized polypeptide chains; member of the HSP70 family; homolog of SSB1<ref name='S000049549'>Craig EA, et al. (1993) Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol Rev 57(2):402-14 {{SGDpaper|S000049549}} PMID 8336673</ref><ref name='S000082012'>Huang P, et al. (2005) The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol 12(6):497-504 {{SGDpaper|S000082012}} PMID 15908962</ref><ref name='S000080473'>Kim SY and Craig EA (2005) Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone ssb or zuo1 to cations, including aminoglycosides. Eukaryot Cell 4(1):82-9 {{SGDpaper|S000080473}} PMID 15643063</ref><ref name='S000052276'>Lopez-Buesa P, et al. (1998) The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proc Natl Acad Sci U S A 95(26):15253-8 |
− | + | {{SGDpaper|S000052276}} PMID 9860955</ref> | |
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==Community Commentary== | ==Community Commentary== | ||
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+ | 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> | ||
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==References== | ==References== | ||
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Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
Systematic name | YNL209W |
Gene name | SSB2 |
Aliases | YG103 |
Feature type | ORF, Verified |
Coordinates | Chr XIV:252059..253900 |
Primary SGDID | S000005153 |
Description of YNL209W: Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in the folding of newly-synthesized polypeptide chains; member of the HSP70 family; homolog of SSB1[1][2][3][4]
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Contents
Community Commentary
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References
See Help:References on how to add references
- ↑ Craig EA, et al. (1993) Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol Rev 57(2):402-14 SGD PMID 8336673
- ↑ Huang P, et al. (2005) The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol 12(6):497-504 SGD PMID 15908962
- ↑ Kim SY and Craig EA (2005) Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone ssb or zuo1 to cations, including aminoglycosides. Eukaryot Cell 4(1):82-9 SGD PMID 15643063
- ↑ Lopez-Buesa P, et al. (1998) The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proc Natl Acad Sci U S A 95(26):15253-8 SGD PMID 9860955
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