PMID:9190831: Difference between revisions

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<span style = 'font-size: large'> '''Bibikov, SI, Biran, R, Rudd, KE and Parkinson, JS'''  (1997) A signal transducer for aerotaxis in Escherichia coli.''J. Bacteriol.'' '''179''':4075-9</span>
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!align=left  |Citation
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'''Bibikov, SI, Biran, R, Rudd, KE and Parkinson, JS'''  (1997) A signal transducer for aerotaxis in Escherichia coli. ''J. Bacteriol.'' '''179''':4075-9
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!align=left  |Abstract
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The newly discovered aer locus of Escherichia coli encodes a 506-residue protein with an N terminus that resembles the NifL aerosensor and a C terminus that resembles the flagellar signaling domain of methyl-accepting chemoreceptors. Deletion mutants lacking a functional Aer protein failed to congregate around air bubbles or follow oxygen gradients in soft agar plates. Membranes with overexpressed Aer protein also contained high levels of noncovalently associated flavin adenine dinucleotide (FAD). We propose that Aer is a flavoprotein that mediates positive aerotactic responses in E. coli. Aer may use its FAD prosthetic group as a cellular redox sensor to monitor environmental oxygen levels.
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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=9190831 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC179224 PMC179224]


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|{{TableHeadingColor}} |'''Abstract''' || The newly discovered aer locus of Escherichia coli encodes a 506-residue protein with an N terminus that resembles the NifL aerosensor and a C terminus that resembles the flagellar signaling domain of methyl-accepting chemoreceptors. Deletion mutants lacking a functional Aer protein failed to congregate around air bubbles or follow oxygen gradients in soft agar plates. Membranes with overexpressed Aer protein also contained high levels of noncovalently associated flavin adenine dinucleotide (FAD). We propose that Aer is a flavoprotein that mediates positive aerotactic responses in E. coli. Aer may use its FAD prosthetic group as a cellular redox sensor to monitor environmental oxygen levels.
!align=left  |Keywords
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Bacterial Proteins/physiology; Escherichia coli/physiology; Flavoproteins/physiology; Oxidation-Reduction; Oxygen; Signal Transduction
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9190831 PubMed]
 
[http://www.ncbi.nlm.nih.gov/entrez/utils/fref.fcgi?PrId=3494&itool=AbstractPlus-nondef&uid=9190831&db=pubmed&url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=9190831 Full text]
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==Annotations {{HelpIcon|Help:Literature}}==
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
==EcoliWiki Links {{HelpIcon|Help:Literature}} ==

Latest revision as of 04:57, 15 September 2013

Citation

Bibikov, SI, Biran, R, Rudd, KE and Parkinson, JS (1997) A signal transducer for aerotaxis in Escherichia coli. J. Bacteriol. 179:4075-9

Abstract

The newly discovered aer locus of Escherichia coli encodes a 506-residue protein with an N terminus that resembles the NifL aerosensor and a C terminus that resembles the flagellar signaling domain of methyl-accepting chemoreceptors. Deletion mutants lacking a functional Aer protein failed to congregate around air bubbles or follow oxygen gradients in soft agar plates. Membranes with overexpressed Aer protein also contained high levels of noncovalently associated flavin adenine dinucleotide (FAD). We propose that Aer is a flavoprotein that mediates positive aerotactic responses in E. coli. Aer may use its FAD prosthetic group as a cellular redox sensor to monitor environmental oxygen levels.

Links

PubMed PMC179224

Keywords

Bacterial Proteins/physiology; Escherichia coli/physiology; Flavoproteins/physiology; Oxidation-Reduction; Oxygen; Signal Transduction

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