Difference between revisions of "YLL024C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003947 YLL024C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003947 YLL024C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''SSA2 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''SSA2 ''
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'''Description of YLL024C:''' ATP binding protein involved in protein folding and vacuolar import of proteins; member of heat shock protein 70 (HSP70) family; associated with the chaperonin-containing T-complex; present in the cytoplasm, vacuolar membrane and cell wall<ref name='S000049670'>Brown CR, et al. (2000) The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles. J Cell Biol 150(1):65-76 {{SGDpaper|S000049670}} PMID 10893257</ref><ref name='S000080727'>Kabir MA, et al. (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39 {{SGDpaper|S000080727}} PMID 15704212</ref><ref name='S000043439'>Lopez-Ribot JL and Chaffin WL (1996) Members of the Hsp70 family of proteins in the cell wall of Saccharomyces cerevisiae. J Bacteriol 178(15):4724-6 {{SGDpaper|S000043439}} PMID 8755907</ref><ref name='S000047102'>Satyanarayana C, et al. (2000) Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole. FEBS Lett 470(3):232-8 {{SGDpaper|S000047102}} PMID 10745074</ref><ref name='S000049179'>Unno K, et al. (1997) Role of Hsp70 subfamily, Ssa, in protein folding in yeast cells, seen in luciferase-transformed ssa mutants. Biol Pharm Bull 20(12):1240-4
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'''Description of YLL024C:''' ATP binding protein involved in protein folding and vacuolar import of proteins; member of heat shock protein 70 (HSP70) family; associated with the chaperonin-containing T-complex; present in the cytoplasm, vacuolar membrane and cell wall; 98% identical with Ssa1p, but subtle differences between the two proteins provide functional specificity with respect to propagation of yeast [URE3] prions and vacuolar-mediated degradations of gluconeogenesis enzymes<ref name='S000049670'>Brown CR, et al. (2000) The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles. J Cell Biol 150(1):65-76 {{SGDpaper|S000049670}} PMID 10893257</ref><ref name='S000080727'>Kabir MA, et al. (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39 {{SGDpaper|S000080727}} PMID 15704212</ref><ref name='S000043439'>Lopez-Ribot JL and Chaffin WL (1996) Members of the Hsp70 family of proteins in the cell wall of Saccharomyces cerevisiae. J Bacteriol 178(15):4724-6 {{SGDpaper|S000043439}} PMID 8755907</ref><ref name='S000047102'>Satyanarayana C, et al. (2000) Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole. FEBS Lett 470(3):232-8 {{SGDpaper|S000047102}} PMID 10745074</ref><ref name='S000146266'>Sharma D and Masison DC (2011) Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc Natl Acad Sci U S A () {{SGDpaper|S000146266}} PMID 21808014</ref><ref name='S000049179'>Unno K, et al. (1997) Role of Hsp70 subfamily, Ssa, in protein folding in yeast cells, seen in luciferase-transformed ssa mutants. Biol Pharm Bull 20(12):1240-4
 
  {{SGDpaper|S000049179}} PMID 9448096</ref>
 
  {{SGDpaper|S000049179}} PMID 9448096</ref>
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YLL024C
Gene name SSA2
Aliases YG102
Feature type ORF, Verified
Coordinates Chr XII:97485..95566
Primary SGDID S000003947


Description of YLL024C: ATP binding protein involved in protein folding and vacuolar import of proteins; member of heat shock protein 70 (HSP70) family; associated with the chaperonin-containing T-complex; present in the cytoplasm, vacuolar membrane and cell wall; 98% identical with Ssa1p, but subtle differences between the two proteins provide functional specificity with respect to propagation of yeast [URE3] prions and vacuolar-mediated degradations of gluconeogenesis enzymes[1][2][3][4][5][6]




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References

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  1. Brown CR, et al. (2000) The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles. J Cell Biol 150(1):65-76 SGD PMID 10893257
  2. Kabir MA, et al. (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39 SGD PMID 15704212
  3. Lopez-Ribot JL and Chaffin WL (1996) Members of the Hsp70 family of proteins in the cell wall of Saccharomyces cerevisiae. J Bacteriol 178(15):4724-6 SGD PMID 8755907
  4. Satyanarayana C, et al. (2000) Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole. FEBS Lett 470(3):232-8 SGD PMID 10745074
  5. Sharma D and Masison DC (2011) Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc Natl Acad Sci U S A () SGD PMID 21808014
  6. Unno K, et al. (1997) Role of Hsp70 subfamily, Ssa, in protein folding in yeast cells, seen in luciferase-transformed ssa mutants. Biol Pharm Bull 20(12):1240-4 SGD PMID 9448096

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