Requirement of Negative Residues, Asp 95 and Asp 105, in S2 on Membrane Integration of a Voltage-dependent K<sup>+</sup>Channel, KAT1

Sato, Yoko; Hosoo, Yoshihiro; Sakaguchi, Masao; Uozumi, Nobuyuki

doi:10.1271/bbb.67.923

Cited by 2 publications

(1 citation statement)

References 13 publications

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“…Here we show that KvLm, a novel prokaryotic Kv channel, embodies an incipient voltage sensor design. In KvLm, only three out of eight positions known to be deterministic for folding ( Papazian et al, 1995 ; Tiwari-Woodruff et al, 1997 ; Tiwari-Woodruff et al, 2000 ; Sato et al, 2003a , b ; Myers et al, 2004 ) or sensing ( Stuhmer et al, 1989 ; Papazian et al, 1991 ; Perozo et al, 1992 ; Shao, and Papazian, 1993 ; Perozo et al, 1994 ; Stefani et al, 1994 ; Planells-Cases et al, 1995 ; Aggarwal, and MacKinnon, 1996 ; Seoh et al, 1996 ; Bezanilla, 2000 ; Ahern, and Horn, 2004 ) in eukaryotic voltage sensors are conserved. Yet this sensor is sufficient to confer to the pore module voltage-dependent features comparable to those measured for eukaryotic Kv channels.…”

Section: Introductionmentioning

confidence: 99%

Molecular Template for a Voltage Sensor in a Novel K+ Channel. I. Identification and Functional Characterization of KvLm, a Voltage-gated K+ Channel from Listeria monocytogenes

Santos

Lundby

Zazueta

et al. 2006

The Journal of General Physiology

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The fundamental principles underlying voltage sensing, a hallmark feature of electrically excitable cells, are still enigmatic and the subject of intense scrutiny and controversy. Here we show that a novel prokaryotic voltage-gated K+ (Kv) channel from Listeria monocytogenes (KvLm) embodies a rudimentary, yet robust, sensor sufficient to endow it with voltage-dependent features comparable to those of eukaryotic Kv channels. The most conspicuous feature of the KvLm sequence is the nature of the sensor components: the motif is recognizable; it appears, however, to contain only three out of eight charged residues known to be conserved in eukaryotic Kv channels and accepted to be deterministic for folding and sensing. Despite the atypical sensor sequence, flux assays of KvLm reconstituted in liposomes disclosed a channel pore that is highly selective for K+ and is blocked by conventional Kv channel blockers. Single-channel currents recorded in symmetric K+ solutions from patches of enlarged Escherichia coli (spheroplasts) expressing KvLm showed that channel open probability sharply increases with depolarization, a hallmark feature of Kv channels. The identification of a voltage sensor module in KvLm with a voltage dependence comparable to that of other eukaryotic Kv channels yet encoded by a sequence that departs significantly from the consensus sequence of a eukaryotic voltage sensor establishes a molecular blueprint of a minimal sequence for a voltage sensor.

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Section: Introductionmentioning

confidence: 99%

Molecular Template for a Voltage Sensor in a Novel K+ Channel. I. Identification and Functional Characterization of KvLm, a Voltage-gated K+ Channel from Listeria monocytogenes

Santos

Lundby

Zazueta

et al. 2006

The Journal of General Physiology

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Conserved motifs in voltage-sensing and pore-forming modules of voltage-gated ion channel proteins

Guda

Bourne

Guda

2007

Biochemical and Biophysical Research Communications

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Requirement of Negative Residues, Asp 95 and Asp 105, in S2 on Membrane Integration of a Voltage-dependent K⁺Channel, KAT1

Cited by 2 publications

References 13 publications

Molecular Template for a Voltage Sensor in a Novel K+ Channel. I. Identification and Functional Characterization of KvLm, a Voltage-gated K+ Channel from Listeria monocytogenes

Molecular Template for a Voltage Sensor in a Novel K+ Channel. I. Identification and Functional Characterization of KvLm, a Voltage-gated K+ Channel from Listeria monocytogenes

Conserved motifs in voltage-sensing and pore-forming modules of voltage-gated ion channel proteins

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Requirement of Negative Residues, Asp 95 and Asp 105, in S2 on Membrane Integration of a Voltage-dependent K+Channel, KAT1

Cited by 2 publications

References 13 publications

Molecular Template for a Voltage Sensor in a Novel K+ Channel. I. Identification and Functional Characterization of KvLm, a Voltage-gated K+ Channel from Listeria monocytogenes

Molecular Template for a Voltage Sensor in a Novel K+ Channel. I. Identification and Functional Characterization of KvLm, a Voltage-gated K+ Channel from Listeria monocytogenes

Conserved motifs in voltage-sensing and pore-forming modules of voltage-gated ion channel proteins

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Requirement of Negative Residues, Asp 95 and Asp 105, in S2 on Membrane Integration of a Voltage-dependent K⁺Channel, KAT1