YAL005C - Revision history

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Shuai at 04:18, 22 February 2007

2007-02-22T04:18:01Z

@@ Line 18: / Line 18: @@
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 <br>
-'''Description of YAL005C:''' ATPase involved in protein folding and nuclear localization signal (NLS)-directed nuclear transport; member of heat shock protein 70 (HSP70) family; forms a chaperone complex with Ydj1p; localized to the nucleus, cytoplasm, and cell wall; 98% identical with Ssa2p, 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='S000052334'>Bush GL and Meyer DI (1996) The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. J Cell Biol 135(5):1229-37 {{SGDpaper|S000052334}} PMID 8947547</ref><ref name='S000045677'>Kim S, et al. (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci U S A 95(22):12860-5 {{SGDpaper|S000045677}} PMID 9789005</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='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='S000046800'>Shulga N, et al. (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7 {{SGDpaper|S000046800}} PMID 10347213</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
+'''Description of YAL005C:''' ATPase involved in protein folding and NLS-directed nuclear transport; member of HSP70 family; forms chaperone complex with Ydj1p; localized to nucleus, cytoplasm, and cell wall; 98% identical with Ssa2p, 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; general targeting factor of Hsp104p to prion fibrils<ref name='S000052334'>Bush GL and Meyer DI (1996) The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. J Cell Biol 135(5):1229-37 {{SGDpaper|S000052334}} PMID 8947547</ref><ref name='S000045677'>Kim S, et al. (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci U S A 95(22):12860-5 {{SGDpaper|S000045677}} PMID 9789005</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='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='S000046800'>Shulga N, et al. (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7 {{SGDpaper|S000046800}} PMID 10347213</ref><ref name='S000150450'>Winkler J, et al. (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404 {{SGDpaper|S000150450}} PMID 22869599</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
   {{SGDpaper|S000049386}} PMID 7737974</ref>
 <br>

@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000004 YAL005C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000004 YAL005C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''SSA1 ''

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YAL005C:''' ATPase involved in protein folding and nuclear localization signal (NLS)-directed nuclear transport; member of heat shock protein 70 (HSP70) family; forms a chaperone complex with Ydj1p; localized to the nucleus, cytoplasm, and cell wall<ref name='S000052334'>Bush GL and Meyer DI (1996) The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. J Cell Biol 135(5):1229-37 {{SGDpaper|S000052334}} PMID 8947547</ref><ref name='S000045677'>Kim S, et al. (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci U S A 95(22):12860-5 {{SGDpaper|S000045677}} PMID 9789005</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='S000046800'>Shulga N, et al. (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7 {{SGDpaper|S000046800}} PMID 10347213</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
+'''Description of YAL005C:''' ATPase involved in protein folding and nuclear localization signal (NLS)-directed nuclear transport; member of heat shock protein 70 (HSP70) family; forms a chaperone complex with Ydj1p; localized to the nucleus, cytoplasm, and cell wall; 98% identical with Ssa2p, 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='S000052334'>Bush GL and Meyer DI (1996) The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. J Cell Biol 135(5):1229-37 {{SGDpaper|S000052334}} PMID 8947547</ref><ref name='S000045677'>Kim S, et al. (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci U S A 95(22):12860-5 {{SGDpaper|S000045677}} PMID 9789005</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='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='S000046800'>Shulga N, et al. (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7 {{SGDpaper|S000046800}} PMID 10347213</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
   {{SGDpaper|S000049386}} PMID 7737974</ref>
 <br>

@@ Line 13: / Line 13: @@
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr I:141433..139505
+|nowrap| Chr I:141431..139503
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000000004

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YAL005C:''' ATPase involved in protein folding and nuclear localization signal (NLS)-directed nuclear transport; member of heat shock protein 70 (HSP70) family; forms a chaperone complex with Ydj1p; localized to the nucleus, cytoplasm, and cell wall<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='S000045677'>Kim S, et al. (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci U S A 95(22):12860-5 {{SGDpaper|S000045677}} PMID 9789005</ref><ref name='S000046800'>Shulga N, et al. (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7 {{SGDpaper|S000046800}} PMID 10347213</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9 {{SGDpaper|S000049386}} PMID 7737974</ref><ref name='S000052334'>Bush GL and Meyer DI (1996) The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. J Cell Biol 135(5):1229-37
+'''Description of YAL005C:''' ATPase involved in protein folding and nuclear localization signal (NLS)-directed nuclear transport; member of heat shock protein 70 (HSP70) family; forms a chaperone complex with Ydj1p; localized to the nucleus, cytoplasm, and cell wall<ref name='S000052334'>Bush GL and Meyer DI (1996) The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. J Cell Biol 135(5):1229-37 {{SGDpaper|S000052334}} PMID 8947547</ref><ref name='S000045677'>Kim S, et al. (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci U S A 95(22):12860-5 {{SGDpaper|S000045677}} PMID 9789005</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='S000046800'>Shulga N, et al. (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7 {{SGDpaper|S000046800}} PMID 10347213</ref><ref name='S000049386'>Ziegelhoffer T, et al. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
- {{SGDpaper|S000052334}} PMID 8947547</ref>
+ {{SGDpaper|S000049386}} PMID 7737974</ref>
 <br>
 <br>

← Older revision		Revision as of 04:18, 22 February 2007
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−	~~<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->~~
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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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