Abstract
The pore-forming subunits of canonical voltage-gated sodium and calcium channels are encoded by four repeated domains of six-transmembrane (6TM) segments. We expressed and characterized a bacterial ion channel (NaChBac) from Bacillus halodurans that is encoded by one 6TM segment. The sequence, especially in the pore region, is similar to that of voltage-gated calcium channels. The expressed channel was activated by voltage and was blocked by calcium channel blockers. However, the channel was selective for sodium. The identification of NaChBac as a functionally expressed bacterial voltage-sensitive ion-selective channel provides insight into both voltage-dependent activation and divalent cation selectivity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Bacillus / chemistry*
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Bacillus / genetics
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Bacillus / metabolism
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Bacterial Proteins*
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CHO Cells
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COS Cells
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Calcium / metabolism
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Calcium Channel Blockers / pharmacology
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Calcium Channels / chemistry
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Calcium Channels / metabolism
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Cricetinae
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Dihydropyridines / pharmacology
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Genes, Bacterial
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Ion Channel Gating
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Membrane Potentials
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Molecular Sequence Data
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Molecular Weight
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Open Reading Frames
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Patch-Clamp Techniques
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Protein Structure, Tertiary
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Recombinant Proteins / metabolism
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Sodium / metabolism*
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Sodium Channels / chemistry
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Sodium Channels / genetics*
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Sodium Channels / metabolism*
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Tetrodotoxin / pharmacology
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Transfection
Substances
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Bacterial Proteins
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Calcium Channel Blockers
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Calcium Channels
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Dihydropyridines
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NaChBac protein, bacteria
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Recombinant Proteins
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Sodium Channels
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Tetrodotoxin
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1,4-dihydropyridine
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Sodium
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Calcium