Association of plant K+(in) channels is mediated by conserved C-termini and does not affect subunit assembly

FEBS Lett. 1997 Jun 9;409(2):166-70. doi: 10.1016/s0014-5793(97)00502-4.

Abstract

Inward rectifying potassium (K+(in)) channels play an important role in turgor regulation and ion uptake in higher plants. Here, we report a previously unrecognized feature of these proteins: K+(in) channel C-terminal polypeptides mediate channel protein interactions. Using a C-terminal fragment of potato guard cell K+(in) channel KST1 in a yeast two-hybrid screen two novel putative K+(in) channel proteins (SKT2 and SKT3) were identified by interaction of their C-termini which contained a conserved domain (K(HA)). Interactions were confirmed by Western blot-related assays utilizing K+(in) channel C-termini fused to green fluorescence protein. Although deletion of the K(HA)-domain abolished these interactions, K+(in) currents were still detectable by patch-clamp measurements of insect cells expressing these KST1 mutants, indicating that formation of a functional channel does not depend on this C-terminal domain.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Conserved Sequence*
  • Membrane Potentials
  • Molecular Sequence Data
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism*
  • Plant Proteins / physiology*
  • Potassium Channels / chemistry
  • Potassium Channels / metabolism*
  • Potassium Channels / physiology*
  • Protein Structure, Tertiary
  • Solanum tuberosum
  • Spodoptera / cytology
  • Spodoptera / physiology

Substances

  • Plant Proteins
  • Potassium Channels

Associated data

  • GENBANK/Y09699
  • GENBANK/Y09818