PMID:2154333: Difference between revisions

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<span style = 'font-size: large'> '''Blair, DF and Berg, HC'''  (1990) The MotA protein of E. coli is a proton-conducting component of the flagellar motor.''Cell'' '''60''':439-49</span>
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!align=left  |Citation
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'''No author listed'''  (1990) The MotA protein of E. coli is a proton-conducting component of the flagellar motor. ''Cell'' '''60''':439-49
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!align=left  |Abstract
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A number of mutants of motA, a gene necessary for flagellar rotation in E. coli, were isolated and characterized. Many mutations were dominant, owing to competition between functional and nonfunctional MotA for a limited number of sites on the flagellar motor. A new class of mutant was discovered in which flagellar torque is normal at low speeds but reduced at high speeds. Hydrogen isotope effects on these mutants indicate that MotA catalyzes proton transfer. We confirmed an earlier observation that overproduction of MotA leads to accumulation of the protein in the cytoplasmic membrane and to significant decreases in growth rate. When nonfunctional mutant variants of MotA were overproduced instead, they accumulated in the cytoplasmic membrane, but growth was not impaired. These results also suggest that MotA conducts protons. This was confirmed by measuring the proton permeabilities of vesicles containing wild-type or mutant MotA proteins.
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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=2154333 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || A number of mutants of motA, a gene necessary for flagellar rotation in E. coli, were isolated and characterized. Many mutations were dominant, owing to competition between functional and nonfunctional MotA for a limited number of sites on the flagellar motor. A new class of mutant was discovered in which flagellar torque is normal at low speeds but reduced at high speeds. Hydrogen isotope effects on these mutants indicate that MotA catalyzes proton transfer. We confirmed an earlier observation that overproduction of MotA leads to accumulation of the protein in the cytoplasmic membrane and to significant decreases in growth rate. When nonfunctional mutant variants of MotA were overproduced instead, they accumulated in the cytoplasmic membrane, but growth was not impaired. These results also suggest that MotA conducts protons. This was confirmed by measuring the proton permeabilities of vesicles containing wild-type or mutant MotA proteins.
!align=left  |Keywords
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Alleles; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Membrane/physiology; Cell Movement; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/physiology; Flagella/physiology; Genes, Bacterial; Genes, Dominant; Genotype; Hydroxylamine; Hydroxylamines/pharmacology; Mutation; Phenotype; Plasmids/drug effects; Protons
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2154333 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 19:13, 1 September 2013

Citation

No author listed (1990) The MotA protein of E. coli is a proton-conducting component of the flagellar motor. Cell 60:439-49

Abstract

A number of mutants of motA, a gene necessary for flagellar rotation in E. coli, were isolated and characterized. Many mutations were dominant, owing to competition between functional and nonfunctional MotA for a limited number of sites on the flagellar motor. A new class of mutant was discovered in which flagellar torque is normal at low speeds but reduced at high speeds. Hydrogen isotope effects on these mutants indicate that MotA catalyzes proton transfer. We confirmed an earlier observation that overproduction of MotA leads to accumulation of the protein in the cytoplasmic membrane and to significant decreases in growth rate. When nonfunctional mutant variants of MotA were overproduced instead, they accumulated in the cytoplasmic membrane, but growth was not impaired. These results also suggest that MotA conducts protons. This was confirmed by measuring the proton permeabilities of vesicles containing wild-type or mutant MotA proteins.

Links

PubMed

Keywords

Alleles; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Membrane/physiology; Cell Movement; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/physiology; Flagella/physiology; Genes, Bacterial; Genes, Dominant; Genotype; Hydroxylamine; Hydroxylamines/pharmacology; Mutation; Phenotype; Plasmids/drug effects; Protons

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