A prokaryotic voltage-gated sodium channel.

D Ren, B Navarro, H Xu, L Yue, Q Shi, D E Clapham
Author Information
  1. D Ren: Howard Hughes Medical Institute, Children's Hospital, Harvard Medical School, Enders 1309, 320 Longwood Avenue, Boston, MA 02115, USA.

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.

MeSH Term

Amino Acid Motifs
Amino Acid Sequence
Animals
Bacillus
Bacterial Proteins
CHO Cells
COS Cells
Calcium
Calcium Channel Blockers
Calcium Channels
Cricetinae
Dihydropyridines
Genes, Bacterial
Ion Channel Gating
Membrane Potentials
Molecular Sequence Data
Molecular Weight
Open Reading Frames
Patch-Clamp Techniques
Protein Structure, Tertiary
Recombinant Proteins
Sodium
Sodium Channels
Tetrodotoxin
Transfection

Chemicals

Bacterial Proteins
Calcium Channel Blockers
Calcium Channels
Dihydropyridines
NaChBac protein, bacteria
Recombinant Proteins
Sodium Channels
Tetrodotoxin
1,4-dihydropyridine
Sodium
Calcium

Word Cloud

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