PMID:14740887 - Revision history

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-15T04:22:53Z

change PMID template to TableEdit version

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	'''~~No author listed~~''' (2003) Mutagenesis studies of the F1F0 ATP synthase b subunit membrane domain. ''J. Bioenerg. Biomembr.'' '''35''':389-97		'''Hardy, AW, Grabar, TB, Bhatt, D and Cain, BD''' (2003) Mutagenesis studies of the F1F0 ATP synthase b subunit membrane domain. ''J. Bioenerg. Biomembr.'' '''35''':389-97
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	!align=left \|Abstract		!align=left \|Abstract

imported>Wikientrybot: replace GO_table_reference with annotationlinks

2013-09-01T18:30:39Z

replace GO_table_reference with annotationlinks

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imported>Wikientrybot: change PMID template to TableEdit version

2013-09-01T18:30:39Z

change PMID template to TableEdit version

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	~~<span style~~ = '~~font-size: large~~'> '~~''Hardy, AW, Grabar, TB, Bhatt, D and Cain, BD~~''' (2003) Mutagenesis studies of the F1F0 ATP synthase b subunit membrane domain.''J. Bioenerg. Biomembr.'' '''35''':389-97</~~span>~~		\|-
			!align=left \|Citation
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			'''No author listed''' (2003) Mutagenesis studies of the F1F0 ATP synthase b subunit membrane domain. ''J. Bioenerg. Biomembr.'' '''35''':389-97
			\|-
			!align=left \|Abstract
			\|\|
			A homodimer of b subunits constitutes the peripheral stalk linking the F1 and F0 sectors of the Escherichia coli ATP synthase. Each b subunit has a single-membrane domain. The constraints on the membrane domain have been studied by systematic mutagenesis. Replacement of a segment proximal to the cytoplasmic side of the membrane had minimal impact on F1F0 ATP synthase. However, multiple substitutions on the periplasmic side resulted in defects in assembly of the enzyme complex. These mutants had insufficient oxidative phosphorylation to support growth, and biochemical studies showed little F1F0 ATPase and no detectable ATP-driven proton pumping activity. Expression of the b(N2A,T6A,Q10A) subunit was also oxidative phosphorylation deficient, but the b(N2A,T6A,Q10A) protein was incorporated into an F1F0 complex. Single amino acid substitutions had minimal reductions in F1F0 ATP synthase function. The evidence suggests that the b subunit membrane domain has several sites of interaction contributing to assembly of F0, and that these interactions are strongest on the periplasmic side of the bilayer.
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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=14740887 PubMed]

	~~{\|{{Prettytable}} align = 'center' width= '70%'~~
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	\|~~{{TableHeadingColor}}~~ \|~~'''Abstract'''~~ \|~~\| A homodimer of b subunits constitutes the peripheral stalk linking the F1 and F0 sectors of the~~ Escherichia coli ~~ATP synthase. Each b subunit has a single~~-membrane domain. The constraints on the membrane domain have been studied by systematic mutagenesis. Replacement of a segment proximal to the cytoplasmic side of the membrane had minimal impact on F1F0 ATP synthase. However, multiple substitutions on the periplasmic side resulted in defects in assembly of the enzyme complex. These mutants had insufficient oxidative phosphorylation to support growth, and biochemical studies showed little F1F0 ATPase and no detectable ATP-~~driven proton pumping activity. Expression of the b(N2A~~,T6A,Q10A) subunit was also oxidative phosphorylation deficient, but the b(N2A,T6A,Q10A) protein was incorporated into an F1F0 complex. Single amino acid substitutions had minimal reductions in F1F0 ATP synthase function. The evidence suggests that the b subunit membrane domain has several sites of interaction contributing to assembly of F0, and that these interactions are strongest on the periplasmic side of the bilayer.		!align=left \|Keywords
	~~</noinclude>~~		\|\|
	\|-		Amino Acid Sequence; Cell Membrane/enzymology; Cell Membrane/genetics; Cloning, Molecular; Escherichia coli/enzymology; Escherichia coli/genetics; Mitochondrial Proton-Translocating ATPases/genetics; Mitochondrial Proton-Translocating ATPases/metabolism; Molecular Sequence Data; Mutagenesis/genetics; Oxidative Phosphorylation; Protein Structure, Tertiary; Protein Subunits/metabolism
	\|{{~~TableHeadingColor~~}} ~~nowrap \|'''Links''' \|\| [http~~:~~//www~~.~~ncbi~~.~~nlm.nih.gov/entrez/query.fcgi?cmd~~=~~Retrieve~~&db=~~pubmed~~&~~dopt~~=~~Abstract~~&~~list_uids~~=~~14740887 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

2010-06-17T20:15:01Z

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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.

2010-01-09T04:12:03Z

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

2009-02-20T01:55:16Z

Fix links due to TableEditLinks.php changes.

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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

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127.0.0.1: Edited by wikibot

2008-04-30T12:27:08Z

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127.0.0.1: Edited by wikibot

2008-04-25T22:15:38Z

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=14740887 PubMed]		\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=14740887 PubMed]
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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
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	==Annotations {{HelpIcon\|Help:Literature}}==		==Annotations {{HelpIcon\|Help:Literature}}==
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	==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==		==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==

172.16.48.28: New PMID: Page!

2008-02-06T07:13:51Z

New PMID: Page!

New page

<protect>
{{RightTOC}}

<span style = 'font-size: large'> '''Hardy, AW, Grabar, TB, Bhatt, D and Cain, BD''' (2003) Mutagenesis studies of the F1F0 ATP synthase b subunit membrane domain.''J. Bioenerg. Biomembr.'' '''35''':389-97</span>

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || A homodimer of b subunits constitutes the peripheral stalk linking the F1 and F0 sectors of the Escherichia coli ATP synthase. Each b subunit has a single-membrane domain. The constraints on the membrane domain have been studied by systematic mutagenesis. Replacement of a segment proximal to the cytoplasmic side of the membrane had minimal impact on F1F0 ATP synthase. However, multiple substitutions on the periplasmic side resulted in defects in assembly of the enzyme complex. These mutants had insufficient oxidative phosphorylation to support growth, and biochemical studies showed little F1F0 ATPase and no detectable ATP-driven proton pumping activity. Expression of the b(N2A,T6A,Q10A) subunit was also oxidative phosphorylation deficient, but the b(N2A,T6A,Q10A) protein was incorporated into an F1F0 complex. Single amino acid substitutions had minimal reductions in F1F0 ATP synthase function. The evidence suggests that the b subunit membrane domain has several sites of interaction contributing to assembly of F0, and that these interactions are strongest on the periplasmic side of the bilayer.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=14740887 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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

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

{|class = 'sortable' {{Prettytable}} id='225557'
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|}
</protect>

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

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