Abstract
MVP, a Methanococcus jannaschii voltage-gated potassium channel, was cloned and shown to operate in eukaryotic and prokaryotic cells. Like pacemaker channels, MVP opens on hyperpolarization using S4 voltage sensors like those in classical channels activated by depolarization. The MVP S4 span resembles classical sensors in sequence, charge, topology and movement, traveling inward on hyperpolarization and outward on depolarization (via canaliculi in the protein that bring the extracellular and internal solutions into proximity across a short barrier). Thus, MVP opens with sensors inward indicating a reversal of S4 position and pore state compared to classical channels. Homologous channels in mammals and plants are expected to function similarly.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence / genetics
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Archaea / genetics
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Archaea / metabolism
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Base Sequence / genetics
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Cloning, Molecular
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Cysteine / metabolism
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DNA, Complementary / analysis
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DNA, Complementary / genetics
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Escherichia coli / metabolism*
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Eukaryotic Cells / metabolism*
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Evolution, Molecular
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Membrane Potentials / physiology
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Mesylates / pharmacology
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Methanococcus / metabolism
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Molecular Sequence Data
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Potassium / metabolism
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Potassium / pharmacology
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Potassium Channels, Voltage-Gated / genetics
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Potassium Channels, Voltage-Gated / isolation & purification*
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Potassium Channels, Voltage-Gated / metabolism
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Prokaryotic Cells / metabolism*
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Protein Structure, Tertiary / physiology
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Saccharomyces cerevisiae / metabolism*
Substances
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DNA, Complementary
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Mesylates
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Potassium Channels, Voltage-Gated
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(2-(trimethylammonium)ethyl)methanethiosulfonate
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Cysteine
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Potassium
Associated data
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GENBANK/AF508327
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GENBANK/M77235
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GENBANK/S32816
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RefSeq/NP_001185