PMID:8892829: Difference between revisions

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<span style = 'font-size: large'> '''Sanna, MG and Simon, MI'''  (1996) In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants.''J. Bacteriol.'' '''178''':6275-80</span>
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!align=left  |Citation
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'''No author listed'''  (1996) In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants. ''J. Bacteriol.'' '''178''':6275-80
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!align=left  |Abstract
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Bacterial chemotaxis results from the ability of flagellated bacteria to control the frequency of switching between smooth-swimming and tumbling episodes in response to changes in concentration of extracellular substances. High levels of phosphorylated CheY protein are the intracellular signal for inducing the tumbling mode of swimming. The CheZ protein has been shown to control the level of phosphorylated CheY by regulating its rate of dephosphorylation. To identify functional domains in the CheZ protein, we made mutants by random mutagenesis of the cheZ gene and constructed a series of deletions. The map position and the in vivo and in vitro activity of the resulting gain- or loss-of-function mutant proteins define separate functional domains of the CheZ protein.
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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=8892829 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC178500 PMC178500]


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|{{TableHeadingColor}} |'''Abstract''' || Bacterial chemotaxis results from the ability of flagellated bacteria to control the frequency of switching between smooth-swimming and tumbling episodes in response to changes in concentration of extracellular substances. High levels of phosphorylated CheY protein are the intracellular signal for inducing the tumbling mode of swimming. The CheZ protein has been shown to control the level of phosphorylated CheY by regulating its rate of dephosphorylation. To identify functional domains in the CheZ protein, we made mutants by random mutagenesis of the cheZ gene and constructed a series of deletions. The map position and the in vivo and in vitro activity of the resulting gain- or loss-of-function mutant proteins define separate functional domains of the CheZ protein.
!align=left  |Keywords
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Bacterial Proteins; Binding Sites; Chemotaxis; Escherichia coli/genetics; Escherichia coli/metabolism; Gene Deletion; Membrane Proteins/genetics; Membrane Proteins/metabolism; Mutagenesis; Phenotype
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8892829 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 19:52, 1 September 2013

Citation

No author listed (1996) In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants. J. Bacteriol. 178:6275-80

Abstract

Bacterial chemotaxis results from the ability of flagellated bacteria to control the frequency of switching between smooth-swimming and tumbling episodes in response to changes in concentration of extracellular substances. High levels of phosphorylated CheY protein are the intracellular signal for inducing the tumbling mode of swimming. The CheZ protein has been shown to control the level of phosphorylated CheY by regulating its rate of dephosphorylation. To identify functional domains in the CheZ protein, we made mutants by random mutagenesis of the cheZ gene and constructed a series of deletions. The map position and the in vivo and in vitro activity of the resulting gain- or loss-of-function mutant proteins define separate functional domains of the CheZ protein.

Links

PubMed PMC178500

Keywords

Bacterial Proteins; Binding Sites; Chemotaxis; Escherichia coli/genetics; Escherichia coli/metabolism; Gene Deletion; Membrane Proteins/genetics; Membrane Proteins/metabolism; Mutagenesis; Phenotype

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