A single amino acid gates the KcsA channel

Minako Hirano, Daichi Okuno, Yukiko Onishi, Toru Ide

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The KcsA channel is a proton-Activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel.

Original languageEnglish
Pages (from-to)1537-1540
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume450
Issue number4
DOIs
Publication statusPublished - Aug 8 2014

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pH sensors
Amino Acids
Potassium Channels
Protons
Mutation

Keywords

  • Ion channel
  • KcsA channel
  • pH-dependent gating
  • Rearrangement
  • Single-channel recording

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

A single amino acid gates the KcsA channel. / Hirano, Minako; Okuno, Daichi; Onishi, Yukiko; Ide, Toru.

In: Biochemical and Biophysical Research Communications, Vol. 450, No. 4, 08.08.2014, p. 1537-1540.

Research output: Contribution to journalArticle

Hirano, Minako ; Okuno, Daichi ; Onishi, Yukiko ; Ide, Toru. / A single amino acid gates the KcsA channel. In: Biochemical and Biophysical Research Communications. 2014 ; Vol. 450, No. 4. pp. 1537-1540.
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