Difference between revisions of "PMID:11985727"

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'''McLaggan, D, Jones, MA, Gouesbet, G, Levina, N, Lindey, S, Epstein, W and Booth, IR'''  (2002) Analysis of the kefA2 mutation suggests that KefA is a cation-specific channel involved in osmotic adaptation in Escherichia coli.''Mol. Microbiol.'' '''43''':521-36
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Mechanosensitive channels play an essential role in the regulation of turgor pressure in bacteria. In Escherichia coli, there are multiple mechanosensitive channels that have been characterized genetically: MscL, YggB and KefA. In this report, we describe the cloning of the kefA gene, the organization of the KefA protein and the phenotype of a missense mutation, kefA, which affects the KefA mechanosensitive channel. The altered function of the channel is manifest through increased sensitivity to K+ during growth at low osmolarity and complete inhibition of growth in media containing high K+ concentrations (0.6 M) in the presence of betaine or proline. Growth in high Na+ medium (0.6 M NaCl plus 20 mM K+) is normal. Analysis of the cytoplasmic pools shows that the mutant cannot regulate the K+ content of the cytoplasm when grown in high K+ medium. However, regulation of pools of amino acids is essentially normal and the mutant can accumulate high pools of proline during growth inhibition. The mutant shows increased sensitivity to acid hypo-osmotic shock (transition from neutral to acid pH combined with a reduction in osmolarity). The data are consistent with abnormal regulation of KefA in the presence of high K+ concentrations and either betaine or proline.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11985727 PubMed]
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Acids; Adaptation, Physiological; Bacterial Proteins; Cations; Escherichia coli; Escherichia coli Proteins; Genes, Bacterial; Glutamic Acid; Mutagenesis; Osmolar Concentration; Osmosis; Potassium; Potassium Channels; Proline; Trehalose; Water-Electrolyte Balance
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==Main Points of the Paper ==
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== Materials and Methods Used ==
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==Phenotype Annotations==
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==Notes==
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==References==
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Revision as of 11:08, 28 March 2011

Citation

McLaggan, D, Jones, MA, Gouesbet, G, Levina, N, Lindey, S, Epstein, W and Booth, IR (2002) Analysis of the kefA2 mutation suggests that KefA is a cation-specific channel involved in osmotic adaptation in Escherichia coli.Mol. Microbiol. 43:521-36

Abstract

Mechanosensitive channels play an essential role in the regulation of turgor pressure in bacteria. In Escherichia coli, there are multiple mechanosensitive channels that have been characterized genetically: MscL, YggB and KefA. In this report, we describe the cloning of the kefA gene, the organization of the KefA protein and the phenotype of a missense mutation, kefA, which affects the KefA mechanosensitive channel. The altered function of the channel is manifest through increased sensitivity to K+ during growth at low osmolarity and complete inhibition of growth in media containing high K+ concentrations (0.6 M) in the presence of betaine or proline. Growth in high Na+ medium (0.6 M NaCl plus 20 mM K+) is normal. Analysis of the cytoplasmic pools shows that the mutant cannot regulate the K+ content of the cytoplasm when grown in high K+ medium. However, regulation of pools of amino acids is essentially normal and the mutant can accumulate high pools of proline during growth inhibition. The mutant shows increased sensitivity to acid hypo-osmotic shock (transition from neutral to acid pH combined with a reduction in osmolarity). The data are consistent with abnormal regulation of KefA in the presence of high K+ concentrations and either betaine or proline.

Links

PubMed

Keywords

Acids; Adaptation, Physiological; Bacterial Proteins; Cations; Escherichia coli; Escherichia coli Proteins; Genes, Bacterial; Glutamic Acid; Mutagenesis; Osmolar Concentration; Osmosis; Potassium; Potassium Channels; Proline; Trehalose; Water-Electrolyte Balance

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Main Points of the Paper

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Materials and Methods Used

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Phenotype Annotations

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Species Taxon ID Strain Gene (if known) OMP Phenotype Details Evidence Notes
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Notes

References

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