PMID:2984180: Difference between revisions

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<span style = 'font-size: large'> '''Clegg, DO and Koshland, DE'''  (1985) Identification of a bacterial sensing protein and effects of its elevated expression.''J. Bacteriol.'' '''162''':398-405</span>
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!align=left  |Citation
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'''No author listed'''  (1985) Identification of a bacterial sensing protein and effects of its elevated expression. ''J. Bacteriol.'' '''162''':398-405
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!align=left  |Abstract
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The Escherichia coli flaA gene product (also called cheC) plays a crucial role in switching flagellar rotational direction during chemotactic responses. Wild-type and mutant alleles have been cloned onto plasmid vectors, and the gene product has been identified as a 37,000-dalton protein. The flaA product appeared as a soluble protein in the cytoplasm when overproduced in minicells and maxicells. The protein could not be detected in flagellar basal structures purified from a wild-type strain. To assess the effects of altered flaA expression, the gene was fused to a synthetic tac promoter that could be regulated by the addition of an inducer. Overproduction resulted in strong counterclockwise flagellar rotational bias and partial paralysis of flagellar motors. These results suggest that the flaA protein provides the interface between the flagellar machinery and the chemotaxis signaling system in a motor structure external to the basal body.
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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=2984180 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC219002 PMC219002]


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|{{TableHeadingColor}} |'''Abstract''' || <protect>The Escherichia coli flaA gene product (also called cheC) plays a crucial role in switching flagellar rotational direction during chemotactic responses. Wild-type and mutant alleles have been cloned onto plasmid vectors, and the gene product has been identified as a 37,000-dalton protein. The flaA product appeared as a soluble protein in the cytoplasm when overproduced in minicells and maxicells. The protein could not be detected in flagellar basal structures purified from a wild-type strain. To assess the effects of altered flaA expression, the gene was fused to a synthetic tac promoter that could be regulated by the addition of an inducer. Overproduction resulted in strong counterclockwise flagellar rotational bias and partial paralysis of flagellar motors. These results suggest that the flaA protein provides the interface between the flagellar machinery and the chemotaxis signaling system in a motor structure external to the basal body.</protect>
!align=left  |Keywords
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2984180 PubMed]<br/>
Bacterial Proteins/analysis; Bacterial Proteins/genetics; Bacterial Proteins/physiology; Chemotaxis; Escherichia coli/genetics; Flagella/physiology; Genes, Bacterial; Plasmids
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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{{LitSignificance}}

Revision as of 19:21, 1 September 2013

Citation

No author listed (1985) Identification of a bacterial sensing protein and effects of its elevated expression. J. Bacteriol. 162:398-405

Abstract

The Escherichia coli flaA gene product (also called cheC) plays a crucial role in switching flagellar rotational direction during chemotactic responses. Wild-type and mutant alleles have been cloned onto plasmid vectors, and the gene product has been identified as a 37,000-dalton protein. The flaA product appeared as a soluble protein in the cytoplasm when overproduced in minicells and maxicells. The protein could not be detected in flagellar basal structures purified from a wild-type strain. To assess the effects of altered flaA expression, the gene was fused to a synthetic tac promoter that could be regulated by the addition of an inducer. Overproduction resulted in strong counterclockwise flagellar rotational bias and partial paralysis of flagellar motors. These results suggest that the flaA protein provides the interface between the flagellar machinery and the chemotaxis signaling system in a motor structure external to the basal body.

Links

PubMed PMC219002

Keywords

Bacterial Proteins/analysis; Bacterial Proteins/genetics; Bacterial Proteins/physiology; Chemotaxis; Escherichia coli/genetics; Flagella/physiology; Genes, Bacterial; Plasmids

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Annotations

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