PMID:8021205 - Revision history

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-15T04:52:55Z

change PMID template to TableEdit version

← Older revision		Revision as of 04:52, 15 September 2013
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	!align=left \|Citation		!align=left \|Citation
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	'''~~No author listed~~''' (1994) In vivo studies of the role of SecA during protein export in Escherichia coli. ''J. Bacteriol.'' '''176''':4197-203		'''Chun, SY and Randall, LL''' (1994) In vivo studies of the role of SecA during protein export in Escherichia coli. ''J. Bacteriol.'' '''176''':4197-203
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	!align=left \|Abstract		!align=left \|Abstract

imported>Wikientrybot: replace GO_table_reference with annotationlinks

2013-09-01T19:42:43Z

replace GO_table_reference with annotationlinks

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 ==Annotations {{HelpIcon|Help:Literature}}==
-<!--box uid=63ce1649aab8b3180235b0af7618f667.0.A47aaa216bc317-->
+<annotationlinks/>
 ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-01T19:42:43Z

change PMID template to TableEdit version

← Older revision		Revision as of 19:42, 1 September 2013
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	~~<span style~~ = '~~font-size: large~~'> '~~''Chun, SY and Randall, LL~~''' (1994) In vivo studies of the role of SecA during protein export in Escherichia coli.''J. Bacteriol.'' '''176''':4197-203</~~span>~~		\|-
			!align=left \|Citation
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			'''No author listed''' (1994) In vivo studies of the role of SecA during protein export in Escherichia coli. ''J. Bacteriol.'' '''176''':4197-203
			\|-
			!align=left \|Abstract
			\|\|
			SecA is found in Escherichia coli both tightly associated with the cytoplasmic membrane where it functions as a translocation ATPase during protein export and free in the cytosol (R. J. Cabelli, K. M. Dolan, L. Qian, and D. B. Oliver, J. Biol. Chem. 266:24420-24427, 1991; D. B. Oliver and J. Beckwith, Cell 30:311-319, 1982; W. Wickner, A. J. M. Driessen, and F.-U. Hartl, Annu. Rev. Biochem. 60:101-124, 1991). Here we show that SecA can be immunoprecipitated from the cytosol in complex with both fully elongated and nascent species of the precursor of maltose-binding protein, an exported, periplasmic protein. In addition, under conditions in which the distribution of SecA between the cytosolic and membrane-bound states changes from that normally observed, the distribution of precursor maltose-binding protein changes in parallel. These results support the idea that cytosolic SecA plays a role in export. With the aim of determining the roles of the multiple binding sites for ATP on SecA, we compared the export defect in a culture of E. coli expressing a temperature-sensitive allele of secA with the defect in a culture treated with sodium azide. The results indicate that the mutational change and treatment with sodium azide inhibit export by affecting different steps in the cycle of ATP binding and hydrolysis by SecA.
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			!align=left \|Links
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			[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8021205 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC205629 PMC205629]

	~~{\|{{Prettytable}} align = 'center' width= '70%'~~
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	\|~~{{TableHeadingColor}}~~ \|~~'''Abstract'''~~ \|~~\| SecA is found in~~ Escherichia coli both tightly associated with the cytoplasmic membrane where it functions as a translocation ATPase during protein export and free in the cytosol (R. J. Cabelli, K. M. Dolan, L. Qian, and D. B. Oliver, J. Biol. Chem. 266:24420-24427, 1991; ~~D. B. Oliver and J. Beckwith, Cell 30:311-319, 1982~~; W. Wickner, A. J. M. Driessen, and F.-U. Hartl, Annu. Rev. Biochem. 60:101-124, 1991). Here we show that SecA can be immunoprecipitated from the cytosol in complex with both fully elongated and nascent species of the precursor of maltose-binding protein, an exported, periplasmic protein. In addition, under conditions in which the distribution of SecA between the cytosolic and membrane-bound states changes from that normally observed, the distribution of precursor maltose-binding protein changes in parallel. These results support the idea that cytosolic SecA plays a role in export. With the aim of determining the roles of the multiple binding sites for ATP on SecA, we compared the export defect in a culture of E. coli ~~expressing a temperature~~-sensitive allele of secA with the defect in a culture treated with sodium azide. The results indicate that the mutational change and treatment with sodium azide inhibit export by affecting different steps in the cycle of ATP binding and hydrolysis by SecA.		!align=left \|Keywords
	~~</noinclude>~~		\|\|
	\|-		ATP-Binding Cassette Transporters; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/isolation & purification; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Azides/pharmacology; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Binding Sites; Biological Transport/drug effects; Carrier Proteins/metabolism; Cell Membrane/metabolism; Cytosol/metabolism; Escherichia coli/drug effects; Escherichia coli/metabolism; Escherichia coli Proteins; Maltose-Binding Proteins; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutation; Periplasmic Binding Proteins; Protein Precursors/metabolism; Sodium Azide
	\|{{~~TableHeadingColor~~}} ~~nowrap \|'''Links''' \|\| [http~~:~~//www~~.~~ncbi~~.~~nlm.nih.gov/entrez/query.fcgi?cmd~~=~~Retrieve~~&db=~~pubmed~~&~~dopt~~=~~Abstract~~&~~list_uids~~=~~8021205 PubMed~~]
	~~[http:~~/~~/www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=8021205 Full text]~~		\|- class="tableEdit_footer"
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	\|}		\|}
			<!--box uid=d41d8cd98f00b204e9800998ecf8427e.126759.H522398b34e002-->
	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}

127.0.0.1: /Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php

2010-06-17T21:10:33Z

/Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php

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	!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status		!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

127.0.0.1: Update TableEdit tables.

2010-01-09T04:56:15Z

Update TableEdit tables.

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imported>Wikientrybot: Fix links due to TableEditLinks.php changes.

2009-02-20T06:28:49Z

Fix links due to TableEditLinks.php changes.

← Older revision		Revision as of 06:28, 20 February 2009
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	!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status		!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

	\|-class='sortbottom'		\|-class='sortbottom'
	\|[{{SERVER}}{{SCRIPTPATH}}~~/index.php~~?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.A47aaa216bc317&page=0&pagename={{FULLPAGENAMEE}} edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|		\|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.A47aaa216bc317&page=0&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|
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Joseph at 02:49, 23 May 2008

2008-05-23T02:49:16Z

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	\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8021205 PubMed]		\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8021205 PubMed]
			[http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=8021205 Full text]
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127.0.0.1: Edited by wikibot

2008-04-30T12:54:48Z

Edited by wikibot

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127.0.0.1: Edited by wikibot

2008-04-25T22:35:55Z

Edited by wikibot

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	\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8021205 PubMed]		\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8021205 PubMed]
	\|}		\|}
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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}
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	==Annotations {{HelpIcon\|Help:Literature}}==		==Annotations {{HelpIcon\|Help:Literature}}==
	~~<protect>~~<!--box uid=63ce1649aab8b3180235b0af7618f667.0.A47aaa216bc317-->		<!--box uid=63ce1649aab8b3180235b0af7618f667.0.A47aaa216bc317-->
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	==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==		==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==

74.192.221.37: New PMID: Page!

2008-02-07T06:15:50Z

New PMID: Page!

New page

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<span style = 'font-size: large'> '''Chun, SY and Randall, LL''' (1994) In vivo studies of the role of SecA during protein export in Escherichia coli.''J. Bacteriol.'' '''176''':4197-203</span>

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || SecA is found in Escherichia coli both tightly associated with the cytoplasmic membrane where it functions as a translocation ATPase during protein export and free in the cytosol (R. J. Cabelli, K. M. Dolan, L. Qian, and D. B. Oliver, J. Biol. Chem. 266:24420-24427, 1991; D. B. Oliver and J. Beckwith, Cell 30:311-319, 1982; W. Wickner, A. J. M. Driessen, and F.-U. Hartl, Annu. Rev. Biochem. 60:101-124, 1991). Here we show that SecA can be immunoprecipitated from the cytosol in complex with both fully elongated and nascent species of the precursor of maltose-binding protein, an exported, periplasmic protein. In addition, under conditions in which the distribution of SecA between the cytosolic and membrane-bound states changes from that normally observed, the distribution of precursor maltose-binding protein changes in parallel. These results support the idea that cytosolic SecA plays a role in export. With the aim of determining the roles of the multiple binding sites for ATP on SecA, we compared the export defect in a culture of E. coli expressing a temperature-sensitive allele of secA with the defect in a culture treated with sodium azide. The results indicate that the mutational change and treatment with sodium azide inhibit export by affecting different steps in the cycle of ATP binding and hydrolysis by SecA.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8021205 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

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</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>