PMID:7559452 - Revision history

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-15T04:50:31Z

change PMID template to TableEdit version

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	'''~~No author listed~~''' (1995) Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins. ''J. Biol. Chem.'' '''270''':23097-103		'''Bishop, RE, Penfold, SS, Frost, LS, Höltje, JV and Weiner, JH''' (1995) Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins. ''J. Biol. Chem.'' '''270''':23097-103
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	!align=left \|Abstract		!align=left \|Abstract

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2013-09-01T19:36:06Z

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imported>Wikientrybot: change PMID template to TableEdit version

2013-09-01T19:36:06Z

change PMID template to TableEdit version

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	~~<span style~~ = '~~font-size: large~~'> '~~''Bishop, RE, Penfold, SS, Frost, LS, Höltje, JV and Weiner, JH~~''' (1995) Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins.''J. Biol. Chem.'' '''270''':23097-103</~~span>~~		\|-
			!align=left \|Citation
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			'''No author listed''' (1995) Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins. ''J. Biol. Chem.'' '''270''':23097-103
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			!align=left \|Abstract
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			We report a novel outer membrane lipoprotein of Escherichia coli. DNA sequencing between ampC and sugE at the 94.5 min region of the E. coli chromosome revealed an open reading frame specifying 177 amino acid residues. Primer extension analysis demonstrated that the promoter is activated at the transition between exponential and stationary growth phases under control of the rpoS sigma factor gene, and this was confirmed in vivo by monitoring expression of beta-galactosidase activity from a lacZ translational fusion. The amino acid sequence exhibited 31% identity with human apolipoprotein D (apoD), which is a component of plasma high density lipoprotein and belongs to the eukaryotic family of lipocalins. The bacterial lipocalin (Blc) contained a short deletion of 7 amino acid residues corresponding to a hydrophobic surface loop that is thought to facilitate the physical interaction between apoD and high density lipoprotein. However, Blc exhibited a typical prokaryotic lipoprotein signal peptide at its amino terminus. Overexpression, membrane fractionation, and metabolic labeling with [3H]palmitate demonstrated that Blc is indeed a globomycin-sensitive outer membrane lipoprotein. Blc represents the first bacterial member of the family of lipocalins and may serve a starvation response function in E. coli.
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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=7559452 PubMed]

	~~{\|{{Prettytable}} align = 'center' width= '70%'~~
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	\|~~{{TableHeadingColor}}~~ \|~~'''Abstract'''~~ \|~~\| We report a novel outer membrane lipoprotein of~~ Escherichia coli~~. DNA sequencing between ampC and sugE at the 94.5 min region of the E.~~ coli ~~chromosome revealed an open reading frame specifying 177 amino acid residues. Primer extension analysis demonstrated that the promoter is activated at the transition between exponential and stationary~~ growth ~~phases under control of the rpoS sigma factor gene~~, and this was confirmed in vivo by monitoring expression of beta-galactosidase activity from a lacZ translational fusion. The amino acid sequence exhibited 31% identity with human apolipoprotein D (apoD), which is a component of plasma high density lipoprotein and belongs to the eukaryotic family of lipocalins. The bacterial lipocalin (Blc) contained a short deletion of 7 amino acid residues corresponding to a hydrophobic surface loop that is thought to facilitate the physical interaction between apoD and high density lipoprotein. However, ~~Blc exhibited a typical prokaryotic lipoprotein signal peptide at its amino terminus. Overexpression~~, membrane fractionation, and metabolic labeling with [3H]palmitate demonstrated that Blc is indeed a globomycin-sensitive outer membrane lipoprotein. Blc represents the first bacterial member of the family of lipocalins and may serve a starvation response function in E. coli.		!align=left \|Keywords
	~~</noinclude>~~		\|\|
	\|-		Algorithms; Amino Acid Sequence; Animals; Apolipoproteins/biosynthesis; Apolipoproteins/chemistry; Apolipoproteins/genetics; Apolipoproteins D; Bacterial Outer Membrane Proteins/biosynthesis; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Proteins/genetics; Base Sequence; Chromosomes, Bacterial; DNA Primers; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Genes, Bacterial; Humans; Lipocalins; Lipoproteins/biosynthesis; Lipoproteins/chemistry; Lipoproteins/genetics; Mammals; Membrane Proteins; Molecular Chaperones; Molecular Sequence Data; Open Reading Frames; Protein Structure, Secondary; Recombinant Fusion Proteins/biosynthesis; Recombinant Fusion Proteins/chemistry; Sequence Homology, Amino Acid; Transcription, Genetic
	\|{{~~TableHeadingColor~~}} ~~nowrap \|'''Links''' \|\| [http~~:~~//www~~.~~ncbi~~.~~nlm.nih.gov/entrez/query.fcgi?cmd~~=~~Retrieve~~&db=~~pubmed~~&~~dopt~~=~~Abstract~~&~~list_uids~~=~~7559452 PubMed~~]
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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}

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

2010-06-17T21:03:52Z

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127.0.0.1: Update TableEdit tables.

2010-01-09T04:51:56Z

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

2009-02-20T06:01:07Z

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127.0.0.1: Edited by wikibot

2008-04-30T12:51:44Z

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Pei at 10:07, 30 April 2008

2008-04-30T10:07:54Z

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127.0.0.1: Edited by wikibot

2008-04-25T22:33:33Z

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=7559452 PubMed]		\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7559452 PubMed]
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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
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	==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==		==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==

74.192.221.37: New PMID: Page!

2008-02-07T05:03:21Z

New PMID: Page!

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<span style = 'font-size: large'> '''Bishop, RE, Penfold, SS, Frost, LS, Höltje, JV and Weiner, JH''' (1995) Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins.''J. Biol. Chem.'' '''270''':23097-103</span>

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || We report a novel outer membrane lipoprotein of Escherichia coli. DNA sequencing between ampC and sugE at the 94.5 min region of the E. coli chromosome revealed an open reading frame specifying 177 amino acid residues. Primer extension analysis demonstrated that the promoter is activated at the transition between exponential and stationary growth phases under control of the rpoS sigma factor gene, and this was confirmed in vivo by monitoring expression of beta-galactosidase activity from a lacZ translational fusion. The amino acid sequence exhibited 31% identity with human apolipoprotein D (apoD), which is a component of plasma high density lipoprotein and belongs to the eukaryotic family of lipocalins. The bacterial lipocalin (Blc) contained a short deletion of 7 amino acid residues corresponding to a hydrophobic surface loop that is thought to facilitate the physical interaction between apoD and high density lipoprotein. However, Blc exhibited a typical prokaryotic lipoprotein signal peptide at its amino terminus. Overexpression, membrane fractionation, and metabolic labeling with [3H]palmitate demonstrated that Blc is indeed a globomycin-sensitive outer membrane lipoprotein. Blc represents the first bacterial member of the family of lipocalins and may serve a starvation response function in E. coli.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7559452 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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

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

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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|}
</protect>

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

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