YDL229W - Revision history

SGDwikiBot: Automated import of articles

2012-01-23T14:45:26Z

Automated import of articles

SGDwikiBot: Automated import of articles

2011-02-03T21:05:23Z

Automated import of articles

SGDwikiBot: Automated import of articles

2010-02-25T21:05:18Z

Automated import of articles

SGDwikiBot: Automated import of articles

2009-03-31T21:05:19Z

Automated import of articles

SGDwikiBot: Automated import of articles

2009-01-16T21:05:20Z

Automated import of articles

SGDwikiBot: Automated import of articles

2008-12-19T11:15:52Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-02-27T15:46:04Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-02-21T20:02:05Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-01-30T15:17:49Z

Automated import of articles

SGDwikiBot: Automated import of articles

2007-01-23T15:20:31Z

Automated import of articles

New page

{{PageTop}}
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YDL229W YDL229W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SSB1 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''YG101''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr IV:44066..45907
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p<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='S000068747'>de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28 {{SGDpaper|S000068747}} PMID 11746603</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><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='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='S000041887'>Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105
{{SGDpaper|S000041887}} PMID 1394434</ref>
 
 
 
 

__TOC__
==Community Commentary==
{{CommentaryHelp}}

==References==

{{RefHelp}}

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr IV:44066..45907
+|nowrap| Chr IV:44065..45906
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000002388

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDL229W:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p<ref name='S000041887'>Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105 {{SGDpaper|S000041887}} PMID 1394434</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='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='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><ref name='S000068747'>de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28 {{SGDpaper|S000068747}} PMID 11746603</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
+'''Description of YDL229W:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p<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><ref name='S000041887'>Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105 {{SGDpaper|S000041887}} PMID 1394434</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='S000068747'>de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28
-  {{SGDpaper|S000080473}} PMID 15643063</ref>
+  {{SGDpaper|S000068747}} PMID 11746603</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDL229W:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p<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='S000068747'>de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28 {{SGDpaper|S000068747}} PMID 11746603</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><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='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='S000041887'>Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105
+'''Description of YDL229W:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p<ref name='S000041887'>Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105 {{SGDpaper|S000041887}} PMID 1394434</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='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='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><ref name='S000068747'>de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28 {{SGDpaper|S000068747}} PMID 11746603</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|S000041887}} PMID 1394434</ref>
+  {{SGDpaper|S000080473}} PMID 15643063</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDL229W:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p<ref name='S000041887'>Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105 {{SGDpaper|S000041887}} PMID 1394434</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='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='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><ref name='S000068747'>de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28 {{SGDpaper|S000068747}} PMID 11746603</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='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
+'''Description of YDL229W:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p<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='S000068747'>de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28 {{SGDpaper|S000068747}} PMID 11746603</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><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='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='S000041887'>Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105
-  {{SGDpaper|S000082012}} PMID 15908962</ref>
+  {{SGDpaper|S000041887}} PMID 1394434</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDL229W:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p<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='S000068747'>de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28 {{SGDpaper|S000068747}} PMID 11746603</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><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='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='S000041887'>Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105
+'''Description of YDL229W:''' Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p<ref name='S000041887'>Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105 {{SGDpaper|S000041887}} PMID 1394434</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='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='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><ref name='S000068747'>de Nobel H, et al. (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28 {{SGDpaper|S000068747}} PMID 11746603</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='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|S000041887}} PMID 1394434</ref>
+  {{SGDpaper|S000082012}} PMID 15908962</ref>
 <br>
 <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=S000002388 YDL229W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002388 YDL229W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''SSB1 ''

← Older revision		Revision as of 20:02, 21 February 2007
Line 28:		Line 28:
	{{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>		<protect>

@@ Line 1: / Line 1: @@
 <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN-->
 {{PageTop}}
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
@@ Line 13: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr IV:44066..45907
 |}
 <br>
@@ Line 23: / Line 22: @@
 <br>
 <br>
+<br>
 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}