PMID:9473056: Difference between revisions

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<span style = 'font-size: large'> '''Barak, R, Abouhamad, WN and Eisenbach, M'''  (1998) Both acetate kinase and acetyl coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar rotation in Escherichia coli.''J. Bacteriol.'' '''180''':985-8</span>
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!align=left  |Citation
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'''No author listed'''  (1998) Both acetate kinase and acetyl coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar rotation in Escherichia coli. ''J. Bacteriol.'' '''180''':985-8
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!align=left  |Abstract
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Escherichia coli strains overproducing the response regulator CheY respond to acetate by increasing their clockwise bias of flagellar rotation, even when they lack other chemotaxis proteins. With acetate metabolism mutants, we demonstrate that both acetate kinase and acetyl coenzyme A synthetase are involved in this response. Thus, a response was observed when one of these enzymes was missing but not when both were absent.
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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=9473056 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC106981 PMC106981]


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|{{TableHeadingColor}} |'''Abstract''' || Escherichia coli strains overproducing the response regulator CheY respond to acetate by increasing their clockwise bias of flagellar rotation, even when they lack other chemotaxis proteins. With acetate metabolism mutants, we demonstrate that both acetate kinase and acetyl coenzyme A synthetase are involved in this response. Thus, a response was observed when one of these enzymes was missing but not when both were absent.
!align=left  |Keywords
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Acetate Kinase/metabolism; Acetate-CoA Ligase/metabolism; Acetates/pharmacology; Bacterial Proteins; Chemotaxis/physiology; Escherichia coli/drug effects; Escherichia coli/physiology; Flagella/drug effects; Membrane Proteins/genetics; Membrane Proteins/metabolism; Movement; Mutation; Recombinant Proteins/metabolism; Signal Transduction
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9473056 PubMed]
 
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=9473056&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=9473056 Full text]
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 20:03, 1 September 2013

Citation

No author listed (1998) Both acetate kinase and acetyl coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar rotation in Escherichia coli. J. Bacteriol. 180:985-8

Abstract

Escherichia coli strains overproducing the response regulator CheY respond to acetate by increasing their clockwise bias of flagellar rotation, even when they lack other chemotaxis proteins. With acetate metabolism mutants, we demonstrate that both acetate kinase and acetyl coenzyme A synthetase are involved in this response. Thus, a response was observed when one of these enzymes was missing but not when both were absent.

Links

PubMed PMC106981

Keywords

Acetate Kinase/metabolism; Acetate-CoA Ligase/metabolism; Acetates/pharmacology; Bacterial Proteins; Chemotaxis/physiology; Escherichia coli/drug effects; Escherichia coli/physiology; Flagella/drug effects; Membrane Proteins/genetics; Membrane Proteins/metabolism; Movement; Mutation; Recombinant Proteins/metabolism; Signal Transduction

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