PMID:12374733: Difference between revisions

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<span style = 'font-size: large'> '''Li, Y, Moe, PC, Chandrasekaran, S, Booth, IR and Blount, P'''  (2002) Ionic regulation of MscK, a mechanosensitive channel from Escherichia coli.''EMBO J.'' '''21''':5323-30</span>
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'''Li, Y, Moe, PC, Chandrasekaran, S, Booth, IR and Blount, P'''  (2002) Ionic regulation of MscK, a mechanosensitive channel from Escherichia coli. ''EMBO J.'' '''21''':5323-30
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!align=left  |Abstract
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Three gene products that form independent mechanosensitive channel activities have been identified in Escherichia coli. Two of these, MscL and MscS, play a vital role in allowing the cell to survive acute hypotonic stress. Much less is known of the third protein, MscK (KefA). Here, we characterize the MscK channel activity and compare it with the activity of its structural and functional homologue, MscS. While both show a slight anionic preference, MscK appears to be more sensitive to membrane tension. In addition, MscK, but not MscS activity appears to be regulated by external ionic environment, requiring not only membrane tension but also high concentrations of external K(+), NH(4)(+), Rb(+) or Cs(+) to gate; no activity is observed with Na(+), Li(+) or N-methyl-D-glucamine (NMDG). An MscK gain-of-function mutant gates spontaneously in the presence of K(+) or similar ions, and will gate in the presence of Na(+), Li(+) and NMDG, but only when stimulated by membrane tension. Increased sensitivity and the highly regulated nature of MscK suggest a more specialized physiological role than other bacterial mechanosensitive channels.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12374733 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC129069 PMC129069]


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|{{TableHeadingColor}} |'''Abstract''' || Three gene products that form independent mechanosensitive channel activities have been identified in Escherichia coli. Two of these, MscL and MscS, play a vital role in allowing the cell to survive acute hypotonic stress. Much less is known of the third protein, MscK (KefA). Here, we characterize the MscK channel activity and compare it with the activity of its structural and functional homologue, MscS. While both show a slight anionic preference, MscK appears to be more sensitive to membrane tension. In addition, MscK, but not MscS activity appears to be regulated by external ionic environment, requiring not only membrane tension but also high concentrations of external K(+), NH(4)(+), Rb(+) or Cs(+) to gate; no activity is observed with Na(+), Li(+) or N-methyl-D-glucamine (NMDG). An MscK gain-of-function mutant gates spontaneously in the presence of K(+) or similar ions, and will gate in the presence of Na(+), Li(+) and NMDG, but only when stimulated by membrane tension. Increased sensitivity and the highly regulated nature of MscK suggest a more specialized physiological role than other bacterial mechanosensitive channels.
!align=left  |Keywords
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Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Genes, Bacterial; Ion Channel Gating; Ion Channels/drug effects; Ion Channels/genetics; Ion Channels/metabolism; Mechanotransduction, Cellular; Mutation; Phenotype; Potassium/pharmacology; Sodium/pharmacology
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12374733 PubMed]
 
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Latest revision as of 04:18, 15 September 2013

Citation

Li, Y, Moe, PC, Chandrasekaran, S, Booth, IR and Blount, P (2002) Ionic regulation of MscK, a mechanosensitive channel from Escherichia coli. EMBO J. 21:5323-30

Abstract

Three gene products that form independent mechanosensitive channel activities have been identified in Escherichia coli. Two of these, MscL and MscS, play a vital role in allowing the cell to survive acute hypotonic stress. Much less is known of the third protein, MscK (KefA). Here, we characterize the MscK channel activity and compare it with the activity of its structural and functional homologue, MscS. While both show a slight anionic preference, MscK appears to be more sensitive to membrane tension. In addition, MscK, but not MscS activity appears to be regulated by external ionic environment, requiring not only membrane tension but also high concentrations of external K(+), NH(4)(+), Rb(+) or Cs(+) to gate; no activity is observed with Na(+), Li(+) or N-methyl-D-glucamine (NMDG). An MscK gain-of-function mutant gates spontaneously in the presence of K(+) or similar ions, and will gate in the presence of Na(+), Li(+) and NMDG, but only when stimulated by membrane tension. Increased sensitivity and the highly regulated nature of MscK suggest a more specialized physiological role than other bacterial mechanosensitive channels.

Links

PubMed PMC129069

Keywords

Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Genes, Bacterial; Ion Channel Gating; Ion Channels/drug effects; Ion Channels/genetics; Ion Channels/metabolism; Mechanotransduction, Cellular; Mutation; Phenotype; Potassium/pharmacology; Sodium/pharmacology

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